Proteopedia

1glv: Difference between revisions

← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1glv' size='340' side='right'caption='[[1glv]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='1glv' size='340' side='right'caption='[[1glv]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1glv]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1GLV FirstGlance]. <br>
<table><tr><td colspan='2'>[[1glv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [https://proteopedia.org/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'>[https://en.wikipedia.org/wiki/Glutathione_synthase Glutathione synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.3 6.3.2.3] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1glv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glv OCA], [https://pdbe.org/1glv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1glv RCSB], [https://www.ebi.ac.uk/pdbsum/1glv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1glv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1glv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glv OCA], [https://pdbe.org/1glv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1glv RCSB], [https://www.ebi.ac.uk/pdbsum/1glv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1glv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSHB_ECOLI GSHB_ECOLI]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 17: Line 19:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1glv ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1glv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutathione 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 &gt; 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<ref>PMID:8445637</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1glv" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Glutathione synthetase|Glutathione synthetase]]
*[[Glutathione synthetase|Glutathione synthetase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Glutathione synthase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kato, H]]
[[Category: Kato H]]
[[Category: Katsube, Y]]
[[Category: Katsube Y]]
[[Category: Tanaka, T]]
[[Category: Tanaka T]]
[[Category: Yamaguchi, H]]
[[Category: Yamaguchi H]]
[[Category: Glutathione biosynthesis ligase]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/w/1glv"