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==THREE-DIMENSIONAL STRUCTURE OF THE GLUTATHIONE SYNTHETASE FROM ESCHERICHIA COLI B AT 2.0 ANGSTROMS RESOLUTION== | ==THREE-DIMENSIONAL STRUCTURE OF THE GLUTATHIONE SYNTHETASE FROM ESCHERICHIA COLI B AT 2.0 ANGSTROMS RESOLUTION== | ||
<StructureSection load='1glv' size='340' side='right' caption='[[1glv]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1glv' size='340' side='right' caption='[[1glv]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
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<table><tr><td colspan='2'>[[1glv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLV FirstGlance]. <br> | <table><tr><td colspan='2'>[[1glv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLV FirstGlance]. <br> | ||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_synthase Glutathione synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.3 6.3.2.3] </span></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_synthase Glutathione synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.3 6.3.2.3] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1glv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glv OCA], [http://pdbe.org/1glv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1glv RCSB], [http://www.ebi.ac.uk/pdbsum/1glv PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1glv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glv OCA], [http://pdbe.org/1glv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1glv RCSB], [http://www.ebi.ac.uk/pdbsum/1glv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1glv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1glv" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1glv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:35, 29 November 2017
THREE-DIMENSIONAL STRUCTURE OF THE GLUTATHIONE SYNTHETASE FROM ESCHERICHIA COLI B AT 2.0 ANGSTROMS RESOLUTIONTHREE-DIMENSIONAL STRUCTURE OF THE GLUTATHIONE SYNTHETASE FROM ESCHERICHIA COLI B AT 2.0 ANGSTROMS RESOLUTION
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlutathione synthetase (gamma-L-glutamyl-L-cysteine: glycine ligase (ADP-forming) EC 6.3.2.3: GSHase) catalyzes the synthesis of glutathione from gamma-L-glutamyl-L-cysteine and Gly in the presence of ATP. The enzyme from Escherichia coli is a tetramer with four identical subunits of 316 amino acid residues. The crystal structure of the enzyme has been determined by isomorphous replacement and refined to a 2.0 A resolution. Two regions, Gly164 to Gly167 and Ile226 to Arg241, are invisible on the electron density map. The refined model of the subunit includes 296 amino acid residues and 107 solvent molecules. The crystallographic R-factor is 18.6% for 17.914 reflections with F > 3 sigma between 6.0 A and 2.0 A. The structure consists of three domains: the N-terminal, central, and C-terminal domains. In the tetrameric molecule, two subunits that are in close contact form a tight dimer, two tight dimers forming a tetramer with two solvent regions. The ATP molecule is located in the cleft between the central and C-terminal domains. The ATP binding site is surrounded by two sets of the structural motif that belong to those respective domains. Each motif consists of an anti-parallel beta-sheet and a glycine-rich loop. Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution.,Yamaguchi H, Kato H, Hata Y, Nishioka T, Kimura A, Oda J, Katsube Y J Mol Biol. 1993 Feb 20;229(4):1083-100. PMID:8445637[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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