The Experts below are selected from a list of 297 Experts worldwide ranked by ideXlab platform
Bauke W Dijkstra - One of the best experts on this subject based on the ideXlab platform.
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identification of the mg2 binding site in the p type atpase and phosphatase members of the had haloacid dehalogenase superfamily by structural similarity to the response Regulator Protein chey
Biochemical Journal, 1999Co-Authors: Ivo S Ridder, Bauke W DijkstraAbstract:The large HAD (haloacid dehalogenase) superfamily of hydrolases comprises P-type ATPases, phosphatases, epoxide hydrolases and L-2-haloacid dehalogenases. A comparison of the three-dimensional structure of L-2-haloacid dehalogenase with that of the response Regulator Protein CheY allowed the assignment of a conserved pair of aspartate residues as the Mg2+-binding site in the P-type ATPase and phosphatase members of the superfamily, From the resulting model of the active site, a conserved serine/threonine residue is suggested to be involved in phosphate binding, and a mechanism comprising a phosphoaspartate intermediate is postulated.
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research communication identification of the mg 2 binding site in the p type atpase and phosphatase members of the had haloacid dehalogenase superfamily by structural similarity to the response Regulator Protein chey
1999Co-Authors: Ivo S Ridder, Bauke W DijkstraAbstract:The large HAD (haloacid dehalogenase) superfamily of hydrolases comprises P-type ATPases, phosphatases, epoxide hydrolases and l-2-haloacid dehalogenases. A comparison of the three-dimensional structure of l-2-haloacid dehalogenase with that of the response Regulator Protein CheY allowed the assignment of a conserved pair of aspartate residues as the Mg#+binding site in the P-type ATPase and phosphatase members of
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RESEARCH COMMUNICATION Identification of the Mg 2 +-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response Regulator Protein CheY
1999Co-Authors: Ivo S Ridder, Bauke W DijkstraAbstract:The large HAD (haloacid dehalogenase) superfamily of hydrolases comprises P-type ATPases, phosphatases, epoxide hydrolases and l-2-haloacid dehalogenases. A comparison of the three-dimensional structure of l-2-haloacid dehalogenase with that of the response Regulator Protein CheY allowed the assignment of a conserved pair of aspartate residues as the Mg#+binding site in the P-type ATPase and phosphatase members of
John F Barrett - One of the best experts on this subject based on the ideXlab platform.
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Protein structure determination using a combination of comparative modeling and NMR spectroscopy. Application to the response Regulator Protein, Spo0F.
Journal of medicinal chemistry, 1997Co-Authors: Brent L. Podlogar, Gregory C. Leo, Patricia A. Mcdonnell, Deborah A. Loughney, Gary W. Caldwell, John F BarrettAbstract:A practical combination of comparative modeling and NMR spectroscopy was used to generate a three-dimensional structure of the response Regulator Protein, Spo0F. The backbone structure obtained compares to the Spo0F Y13S mutant X-ray structure with an rmsd of 2.0 A. We provide results which suggest that structures obtained by this method are suitable for drug discovery. The results of the GRID and DOCK methods as applied to the model and X-ray structures of Spo0F are remarkably similar and tend to suggest the same design conclusions. This trend is illustrated by these same techniques applied to two experimentally derived structures of the analogous Protein, CheY, which exhibit a pairwise rmsdBB on the same order as that found for the two Spo0F structures.
Ivo S Ridder - One of the best experts on this subject based on the ideXlab platform.
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identification of the mg2 binding site in the p type atpase and phosphatase members of the had haloacid dehalogenase superfamily by structural similarity to the response Regulator Protein chey
Biochemical Journal, 1999Co-Authors: Ivo S Ridder, Bauke W DijkstraAbstract:The large HAD (haloacid dehalogenase) superfamily of hydrolases comprises P-type ATPases, phosphatases, epoxide hydrolases and L-2-haloacid dehalogenases. A comparison of the three-dimensional structure of L-2-haloacid dehalogenase with that of the response Regulator Protein CheY allowed the assignment of a conserved pair of aspartate residues as the Mg2+-binding site in the P-type ATPase and phosphatase members of the superfamily, From the resulting model of the active site, a conserved serine/threonine residue is suggested to be involved in phosphate binding, and a mechanism comprising a phosphoaspartate intermediate is postulated.
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research communication identification of the mg 2 binding site in the p type atpase and phosphatase members of the had haloacid dehalogenase superfamily by structural similarity to the response Regulator Protein chey
1999Co-Authors: Ivo S Ridder, Bauke W DijkstraAbstract:The large HAD (haloacid dehalogenase) superfamily of hydrolases comprises P-type ATPases, phosphatases, epoxide hydrolases and l-2-haloacid dehalogenases. A comparison of the three-dimensional structure of l-2-haloacid dehalogenase with that of the response Regulator Protein CheY allowed the assignment of a conserved pair of aspartate residues as the Mg#+binding site in the P-type ATPase and phosphatase members of
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RESEARCH COMMUNICATION Identification of the Mg 2 +-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response Regulator Protein CheY
1999Co-Authors: Ivo S Ridder, Bauke W DijkstraAbstract:The large HAD (haloacid dehalogenase) superfamily of hydrolases comprises P-type ATPases, phosphatases, epoxide hydrolases and l-2-haloacid dehalogenases. A comparison of the three-dimensional structure of l-2-haloacid dehalogenase with that of the response Regulator Protein CheY allowed the assignment of a conserved pair of aspartate residues as the Mg#+binding site in the P-type ATPase and phosphatase members of
Brent L. Podlogar - One of the best experts on this subject based on the ideXlab platform.
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Protein structure determination using a combination of comparative modeling and NMR spectroscopy. Application to the response Regulator Protein, Spo0F.
Journal of medicinal chemistry, 1997Co-Authors: Brent L. Podlogar, Gregory C. Leo, Patricia A. Mcdonnell, Deborah A. Loughney, Gary W. Caldwell, John F BarrettAbstract:A practical combination of comparative modeling and NMR spectroscopy was used to generate a three-dimensional structure of the response Regulator Protein, Spo0F. The backbone structure obtained compares to the Spo0F Y13S mutant X-ray structure with an rmsd of 2.0 A. We provide results which suggest that structures obtained by this method are suitable for drug discovery. The results of the GRID and DOCK methods as applied to the model and X-ray structures of Spo0F are remarkably similar and tend to suggest the same design conclusions. This trend is illustrated by these same techniques applied to two experimentally derived structures of the analogous Protein, CheY, which exhibit a pairwise rmsdBB on the same order as that found for the two Spo0F structures.
Takeshi Mizuno - One of the best experts on this subject based on the ideXlab platform.
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A novel sensor-Regulator Protein that belongs to the homologous family of signal-transduction Proteins involved in adaptive responses in Escherichia coli.
Molecular microbiology, 1992Co-Authors: Shinobu Nagasawa, Shin-ichi Tokishita, Hirofumi Aiba, Takeshi MizunoAbstract:Summary Expression of the Escherichia coli outer membrane porins, OmpC and OmpF, is regulated in response to changes in the medium osmolarity through the functions of the Regulatory factors, EnvZ and OmpR. A 3.0 kilobase pair DNA fragment cloned from E. coli is able phenotypically to suppress the defect in ompC and ompF expression caused by an envZ deletion mutation, provided that a certain gene located in this fragment is expressed on a high copy-number plasmid. Nucleotide sequencing revealed that the putative gene encodes a Protein of 102452 Da. The deduced amino acid sequence of the Protein shows a high degree of homology to those of both EnvZ and OmpR, i.e. it contains both a sensory kinase domain’ and a ‘response Regulator domain’ in its primary amino acid sequence. The Protein identified in this study is probably a novel member of the homologous family of Proteins involved in bacterial adaptive responses. Hence, the gene encoding this novel sensor-Regulator Protein was designated as barA (bacterial adaptive responses) and mapped at 60 min on the E. coli genetic map. The BarA Protein in isolated membranes was demonstrated in vitro to undergo phosphorylation in the presence of ATP.