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| | <StructureSection load='2glt' size='340' side='right'caption='[[2glt]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2glt' size='340' side='right'caption='[[2glt]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2glt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_(strain_b) Escherichia coli (strain b)]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1glt 1glt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GLT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2glt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_B Escherichia coli B]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1glt 1glt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GLT FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSHII ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37762 Escherichia coli (strain B)])</td></tr> | + | </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=2glt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glt OCA], [https://pdbe.org/2glt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2glt RCSB], [https://www.ebi.ac.uk/pdbsum/2glt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2glt ProSAT]</span></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>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2glt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glt OCA], [https://pdbe.org/2glt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2glt RCSB], [https://www.ebi.ac.uk/pdbsum/2glt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2glt 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]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glutathione synthase]] | + | [[Category: Escherichia coli B]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kato, H]] | + | [[Category: Kato H]] |
| - | [[Category: Katsube, Y]] | + | [[Category: Katsube Y]] |
| - | [[Category: Matsuda, K]] | + | [[Category: Matsuda K]] |
| - | [[Category: Nishioka, T]] | + | [[Category: Nishioka T]] |
| - | [[Category: Oda, J]] | + | [[Category: Oda J]] |
| - | [[Category: Yamaguchi, H]] | + | [[Category: Yamaguchi H]] |
| - | [[Category: Biosynthesis]]
| + | |
| - | [[Category: Glutathione biosynthesis ligase]]
| + | |
| - | [[Category: Ligase]]
| + | |
| Structural highlights
Function
GSHB_ECOLI
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 PubMed
The crystal structure of Escherichia coli B glutathione synthetase (GSHase) has been determined at the optimal catalytic condition pH 7.5. The most significant structural difference from the structure at pH 6.0 is the movement of the central domain towards the N-terminal domain almost as a rigid body. As a result of this movement, new interdomain and intersubunit polar interactions are formed which stabilize the dimeric structure further. The structure of GSHase at optimal pH was compared with 294 other known protein structures in terms of the spatial arrangements of secondary structural elements. Three enzymes (D-alanine: D-alanine ligase, succinyl-CoA synthetase and the biotin carboxylase subunit of acetyl-CoA carboxylase) were found to have structures similar to the ATP-binding site of GSHase, which extends across two domains. The ATP-binding sites in these four enzymes are composed of two antiparallel beta-sheets and are different from the classic mononucleotide-binding fold. Except for these proteins, no significant structural similarity was detected between GSHase and the other ATP-binding proteins. A structural motif in the N-terminal domain of GSHase has been found to be similar to the NAD-binding fold. This structural motif is shared by a number of other proteins that bind various negatively charged molecules.
Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins.,Matsuda K, Mizuguchi K, Nishioka T, Kato H, Go N, Oda J Protein Eng. 1996 Dec;9(12):1083-92. PMID:9010922[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matsuda K, Mizuguchi K, Nishioka T, Kato H, Go N, Oda J. Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins. Protein Eng. 1996 Dec;9(12):1083-92. PMID:9010922
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