2glt
From Proteopedia
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| - | [[Image:2glt.gif|left|200px]] | + | [[Image:2glt.gif|left|200px]] |
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| - | '''STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0.''' | + | {{Structure |
| + | |PDB= 2glt |SIZE=350|CAPTION= <scene name='initialview01'>2glt</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= GSHII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GLT is a [ | + | 2GLT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1GLT. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLT OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9010922 9010922] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Glutathione synthase]] | [[Category: Glutathione synthase]] | ||
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[[Category: glutathione biosynthesis ligase]] | [[Category: glutathione biosynthesis ligase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:06:11 2008'' |
Revision as of 15:06, 20 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | GSHII (Escherichia coli) | ||||||
| Activity: | Glutathione synthase, with EC number 6.3.2.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0.
Overview
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.
About this Structure
2GLT is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1GLT. Full crystallographic information is available from OCA.
Reference
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
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