The Experts below are selected from a list of 55149 Experts worldwide ranked by ideXlab platform
Sherry L. Mowbray - One of the best experts on this subject based on the ideXlab platform.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R G Zhang, Evalena C Andersson, Ekaterina Evdokimova, S Beasley, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, Rfree 23.7%). RpiA exhibits an α/β/(α/β)/β/α fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R Zhang, Ekaterina Evdokimova, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Evalena C Andersso, S Easley, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, R(free) 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
A M Edwards - One of the best experts on this subject based on the ideXlab platform.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R G Zhang, Evalena C Andersson, Ekaterina Evdokimova, S Beasley, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, Rfree 23.7%). RpiA exhibits an α/β/(α/β)/β/α fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R Zhang, Ekaterina Evdokimova, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Evalena C Andersso, S Easley, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, R(free) 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
Tatiana Skarina - One of the best experts on this subject based on the ideXlab platform.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R G Zhang, Evalena C Andersson, Ekaterina Evdokimova, S Beasley, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, Rfree 23.7%). RpiA exhibits an α/β/(α/β)/β/α fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R Zhang, Ekaterina Evdokimova, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Evalena C Andersso, S Easley, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, R(free) 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
Alexei Savchenko - One of the best experts on this subject based on the ideXlab platform.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R G Zhang, Evalena C Andersson, Ekaterina Evdokimova, S Beasley, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, Rfree 23.7%). RpiA exhibits an α/β/(α/β)/β/α fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R Zhang, Ekaterina Evdokimova, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Evalena C Andersso, S Easley, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, R(free) 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
Andrzej Joachimiak - One of the best experts on this subject based on the ideXlab platform.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R G Zhang, Evalena C Andersson, Ekaterina Evdokimova, S Beasley, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, Rfree 23.7%). RpiA exhibits an α/β/(α/β)/β/α fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
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structure of escherichia coli ribose 5 phosphate isomerase a ubiquitous enzyme of the pentose phosphate pathway and the calvin cycle
Structure, 2003Co-Authors: R Zhang, Ekaterina Evdokimova, Cheryl H. Arrowsmith, A M Edwards, Tatiana Skarina, Alexei Savchenko, Andrzej Joachimiak, Evalena C Andersso, S Easley, Sherry L. MowbrayAbstract:Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, R(free) 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for Acid-Base Catalysis is proposed.
