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Masaru Tanokura - One of the best experts on this subject based on the ideXlab platform.
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spec...
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spectroscopy. The main body (Glu13−Asp97) of oryzacystatin-I is well-defined and consists of an α-helix and a five-stranded antiparallel β-sheet, while the N- and C-terminal regions (Ser2−Val12 and Ala98−Ala102) are less defined. The helix-sheet architechture of oryzacystatin-I is stabilized by a hydrophobic cluster formed between the α-helix and the β-sheet and is considerably similar to that of monellin, a sweet-tasting protein from an African berry, as well as those of the animal cystatins studied, e.g., chicken egg white cystatin and human stefins A and B (also referred to as human cystatins A and B). Detailed structural comparison indicates that oryzacystatin-I is more similar to chicken cystatin, which belongs to the type-2 animal cystatins, than to human stefins A and B, which belong to the type-1 animal cyst...
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crystallization and preliminary x ray diffraction studies of a rice Cysteine Proteinase Inhibitor oryzacystatin i
Journal of Biochemistry, 1998Co-Authors: Norio Kudo, Keiko Abe, Soichi Arai, Makoto Nishiyama, Hiroshi Sasaki, Masaru TanokuraAbstract:Oryzacystatin-I from rice seeds was overexpressed in Escherichia coli, purified, and crystallized by the sitting-drop vapor diffusion method. Crystals obtained with 2-methyl-2,4-pentanediol as a precipitant exhibited space group I4122, with unit cell parameters of a = b = 100.0 A, c = 54.2 A, and diffracted up to 2.8 A resolution at 100 K. The crystals have one molecule per asymmetric unit.
Keiko Abe - One of the best experts on this subject based on the ideXlab platform.
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spec...
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spectroscopy. The main body (Glu13−Asp97) of oryzacystatin-I is well-defined and consists of an α-helix and a five-stranded antiparallel β-sheet, while the N- and C-terminal regions (Ser2−Val12 and Ala98−Ala102) are less defined. The helix-sheet architechture of oryzacystatin-I is stabilized by a hydrophobic cluster formed between the α-helix and the β-sheet and is considerably similar to that of monellin, a sweet-tasting protein from an African berry, as well as those of the animal cystatins studied, e.g., chicken egg white cystatin and human stefins A and B (also referred to as human cystatins A and B). Detailed structural comparison indicates that oryzacystatin-I is more similar to chicken cystatin, which belongs to the type-2 animal cystatins, than to human stefins A and B, which belong to the type-1 animal cyst...
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crystallization and preliminary x ray diffraction studies of a rice Cysteine Proteinase Inhibitor oryzacystatin i
Journal of Biochemistry, 1998Co-Authors: Norio Kudo, Keiko Abe, Soichi Arai, Makoto Nishiyama, Hiroshi Sasaki, Masaru TanokuraAbstract:Oryzacystatin-I from rice seeds was overexpressed in Escherichia coli, purified, and crystallized by the sitting-drop vapor diffusion method. Crystals obtained with 2-methyl-2,4-pentanediol as a precipitant exhibited space group I4122, with unit cell parameters of a = b = 100.0 A, c = 54.2 A, and diffracted up to 2.8 A resolution at 100 K. The crystals have one molecule per asymmetric unit.
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corn kernel Cysteine Proteinase Inhibitor as a novel cystatin superfamily member of plant origin molecular cloning and expression studies
FEBS Journal, 1992Co-Authors: Makoto Abe, Keiko Abe, Masaharu Kuroda, Soichi AraiAbstract:A full-length cDNA clone for a Cysteine Proteinase Inhibitor (cystatin) was isolated from a lambda gt10 cDNA library of immature corn kernels by screening with a mixture of cDNA inserts for oryzacystatins I and II. The cDNA clone spans 960 base pairs, encoding a 135-amino-acid protein containing a signal peptide fragment. The protein, named corn cystatin I, is considered to be a member of the cystatin superfamily, since it contains the commonly conserved Gln-Val-Val-Ala-Gly region that exists in most known cystatins as a probable binding site and is significantly similar to other cystatins in its overall amino acid sequence. Corn cystatin I expressed in Escherichia coli showed a strong papain-Inhibitory activity. Northern blot analysis showed that the amount of mRNA for corn cystatin I reaches a maximum 2 weeks after flowering and then decreases gradually.
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Papain-Inhibitory activity of oryzacystatin, a rice seed Cysteine Proteinase Inhibitor, depends on the central Gln-Val-Val-Ala-Gly region conserved among cystatin superfamily members.
The Journal of Biochemistry, 1991Co-Authors: Soichi Arai, Hiroto Kondo, Yasufumi Emori, Hirohito Watanabe, Keiko AbeAbstract:Oryzacystatin, a Cysteine Proteinase Inhibitor occurring in rice seeds, contains a particular glycine residue (Gly5) near the NH2-terminal position, and the sequence Gln53-Val54-Val55-Ala56-Gly57 in a central part of the molecule. Both are conserved among most members of the cystatin superfamily. We have found from Escherichia coli expression studies that the NH2-terminal 21 residues of oryzacystatin are not essential for its papain-Inhibitory activity, and that the conserved pentapeptide region may be indispensable [Abe, K., Emori, Y., Kondo, H., Arai, S., & Suzuki, K. (1988) J. Biol. Chem. 263, 7655-7659]. Here we present more detailed data based on quantitative analyses of the Inhibitory activities of NH2- and COOH-terminally truncated oryzacystatin and site-directed mutants at the Gln-Val-Val-Ala-Gly region. The data indicate the following results. (1) The truncated mutants lacking the NH2-terminal 21 residues or the COOH-terminal 11 residues exhibit potent papain-Inhibitory activity equivalent to the activity of wild oryzacystatin. (2) However, neither the mutant lacking the NH2-terminal 38 residues nor that lacking the COOH-terminal 35 residues is completely able to inhibit papain. (3) Site-directed mutants at the Gln residue of the Gln-Val-Val-Ala-Gly region have drastically reduced papain-Inhibitory activities: the Gln----Pro mutant is completely inactive and the Gln----Leu mutant has an approximately 150 times higher Ki value than wild-type oryzacystatin.(ABSTRACT TRUNCATED AT 250 WORDS)
Soichi Arai - One of the best experts on this subject based on the ideXlab platform.
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spec...
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spectroscopy. The main body (Glu13−Asp97) of oryzacystatin-I is well-defined and consists of an α-helix and a five-stranded antiparallel β-sheet, while the N- and C-terminal regions (Ser2−Val12 and Ala98−Ala102) are less defined. The helix-sheet architechture of oryzacystatin-I is stabilized by a hydrophobic cluster formed between the α-helix and the β-sheet and is considerably similar to that of monellin, a sweet-tasting protein from an African berry, as well as those of the animal cystatins studied, e.g., chicken egg white cystatin and human stefins A and B (also referred to as human cystatins A and B). Detailed structural comparison indicates that oryzacystatin-I is more similar to chicken cystatin, which belongs to the type-2 animal cystatins, than to human stefins A and B, which belong to the type-1 animal cyst...
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crystallization and preliminary x ray diffraction studies of a rice Cysteine Proteinase Inhibitor oryzacystatin i
Journal of Biochemistry, 1998Co-Authors: Norio Kudo, Keiko Abe, Soichi Arai, Makoto Nishiyama, Hiroshi Sasaki, Masaru TanokuraAbstract:Oryzacystatin-I from rice seeds was overexpressed in Escherichia coli, purified, and crystallized by the sitting-drop vapor diffusion method. Crystals obtained with 2-methyl-2,4-pentanediol as a precipitant exhibited space group I4122, with unit cell parameters of a = b = 100.0 A, c = 54.2 A, and diffracted up to 2.8 A resolution at 100 K. The crystals have one molecule per asymmetric unit.
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corn kernel Cysteine Proteinase Inhibitor as a novel cystatin superfamily member of plant origin molecular cloning and expression studies
FEBS Journal, 1992Co-Authors: Makoto Abe, Keiko Abe, Masaharu Kuroda, Soichi AraiAbstract:A full-length cDNA clone for a Cysteine Proteinase Inhibitor (cystatin) was isolated from a lambda gt10 cDNA library of immature corn kernels by screening with a mixture of cDNA inserts for oryzacystatins I and II. The cDNA clone spans 960 base pairs, encoding a 135-amino-acid protein containing a signal peptide fragment. The protein, named corn cystatin I, is considered to be a member of the cystatin superfamily, since it contains the commonly conserved Gln-Val-Val-Ala-Gly region that exists in most known cystatins as a probable binding site and is significantly similar to other cystatins in its overall amino acid sequence. Corn cystatin I expressed in Escherichia coli showed a strong papain-Inhibitory activity. Northern blot analysis showed that the amount of mRNA for corn cystatin I reaches a maximum 2 weeks after flowering and then decreases gradually.
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Papain-Inhibitory activity of oryzacystatin, a rice seed Cysteine Proteinase Inhibitor, depends on the central Gln-Val-Val-Ala-Gly region conserved among cystatin superfamily members.
The Journal of Biochemistry, 1991Co-Authors: Soichi Arai, Hiroto Kondo, Yasufumi Emori, Hirohito Watanabe, Keiko AbeAbstract:Oryzacystatin, a Cysteine Proteinase Inhibitor occurring in rice seeds, contains a particular glycine residue (Gly5) near the NH2-terminal position, and the sequence Gln53-Val54-Val55-Ala56-Gly57 in a central part of the molecule. Both are conserved among most members of the cystatin superfamily. We have found from Escherichia coli expression studies that the NH2-terminal 21 residues of oryzacystatin are not essential for its papain-Inhibitory activity, and that the conserved pentapeptide region may be indispensable [Abe, K., Emori, Y., Kondo, H., Arai, S., & Suzuki, K. (1988) J. Biol. Chem. 263, 7655-7659]. Here we present more detailed data based on quantitative analyses of the Inhibitory activities of NH2- and COOH-terminally truncated oryzacystatin and site-directed mutants at the Gln-Val-Val-Ala-Gly region. The data indicate the following results. (1) The truncated mutants lacking the NH2-terminal 21 residues or the COOH-terminal 11 residues exhibit potent papain-Inhibitory activity equivalent to the activity of wild oryzacystatin. (2) However, neither the mutant lacking the NH2-terminal 38 residues nor that lacking the COOH-terminal 35 residues is completely able to inhibit papain. (3) Site-directed mutants at the Gln residue of the Gln-Val-Val-Ala-Gly region have drastically reduced papain-Inhibitory activities: the Gln----Pro mutant is completely inactive and the Gln----Leu mutant has an approximately 150 times higher Ki value than wild-type oryzacystatin.(ABSTRACT TRUNCATED AT 250 WORDS)
Norio Kudo - One of the best experts on this subject based on the ideXlab platform.
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spec...
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spectroscopy. The main body (Glu13−Asp97) of oryzacystatin-I is well-defined and consists of an α-helix and a five-stranded antiparallel β-sheet, while the N- and C-terminal regions (Ser2−Val12 and Ala98−Ala102) are less defined. The helix-sheet architechture of oryzacystatin-I is stabilized by a hydrophobic cluster formed between the α-helix and the β-sheet and is considerably similar to that of monellin, a sweet-tasting protein from an African berry, as well as those of the animal cystatins studied, e.g., chicken egg white cystatin and human stefins A and B (also referred to as human cystatins A and B). Detailed structural comparison indicates that oryzacystatin-I is more similar to chicken cystatin, which belongs to the type-2 animal cystatins, than to human stefins A and B, which belong to the type-1 animal cyst...
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crystallization and preliminary x ray diffraction studies of a rice Cysteine Proteinase Inhibitor oryzacystatin i
Journal of Biochemistry, 1998Co-Authors: Norio Kudo, Keiko Abe, Soichi Arai, Makoto Nishiyama, Hiroshi Sasaki, Masaru TanokuraAbstract:Oryzacystatin-I from rice seeds was overexpressed in Escherichia coli, purified, and crystallized by the sitting-drop vapor diffusion method. Crystals obtained with 2-methyl-2,4-pentanediol as a precipitant exhibited space group I4122, with unit cell parameters of a = b = 100.0 A, c = 54.2 A, and diffracted up to 2.8 A resolution at 100 K. The crystals have one molecule per asymmetric unit.
Koji Nagata - One of the best experts on this subject based on the ideXlab platform.
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spec...
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three dimensional solution structure of oryzacystatin i a Cysteine Proteinase Inhibitor of the rice oryza sativa l japonica
Biochemistry, 2000Co-Authors: Koji Nagata, Keiko Abe, Soichi Arai, Norio Kudo, Masaru TanokuraAbstract:The three-dimensional structure of oryzacystatin-I, a Cysteine Proteinase Inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 °C by 1H and 15N NMR spectroscopy. The main body (Glu13−Asp97) of oryzacystatin-I is well-defined and consists of an α-helix and a five-stranded antiparallel β-sheet, while the N- and C-terminal regions (Ser2−Val12 and Ala98−Ala102) are less defined. The helix-sheet architechture of oryzacystatin-I is stabilized by a hydrophobic cluster formed between the α-helix and the β-sheet and is considerably similar to that of monellin, a sweet-tasting protein from an African berry, as well as those of the animal cystatins studied, e.g., chicken egg white cystatin and human stefins A and B (also referred to as human cystatins A and B). Detailed structural comparison indicates that oryzacystatin-I is more similar to chicken cystatin, which belongs to the type-2 animal cystatins, than to human stefins A and B, which belong to the type-1 animal cyst...
