1chd
From Proteopedia
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| - | [[Image:1chd.jpg|left|200px]] | + | [[Image:1chd.jpg|left|200px]] |
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| - | '''CHEB METHYLESTERASE DOMAIN''' | + | {{Structure |
| + | |PDB= 1chd |SIZE=350|CAPTION= <scene name='initialview01'>1chd</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Protein-glutamate_methylesterase Protein-glutamate methylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.61 3.1.1.61] | ||
| + | |GENE= CHEB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium]) | ||
| + | }} | ||
| + | |||
| + | '''CHEB METHYLESTERASE DOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CHD is a [ | + | 1CHD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHD OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB., West AH, Martinez-Hackert E, Stock AM, J Mol Biol. 1995 Jul 7;250(2):276-90. PMID:[http:// | + | Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB., West AH, Martinez-Hackert E, Stock AM, J Mol Biol. 1995 Jul 7;250(2):276-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7608974 7608974] |
[[Category: Protein-glutamate methylesterase]] | [[Category: Protein-glutamate methylesterase]] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
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[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
| - | ''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 10:24:28 2008'' |
Revision as of 08:24, 20 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | CHEB (Salmonella typhimurium) | ||||||
| Activity: | Protein-glutamate methylesterase, with EC number 3.1.1.61 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHEB METHYLESTERASE DOMAIN
Overview
Signaling activity of bacterial chemotaxis transmembrane receptors is modulated by reversible covalent modification of specific receptor glutamate residues. The level of receptor methylation results from the activities of a specific S-adenosylmethionine-dependent methyltransferase, CheR, and the CheB methylesterase, which catalyzes hydrolysis of receptor glutamine or methylglutamate side-chains to glutamic acid. The CheB methylesterase belongs to a large family of response regulator proteins in which N-terminal regulatory domains control the activities of C-terminal effector domains. The crystal structure of the catalytic domain of the Salmonella typhimurium CheB methylesterase has been determined at 1.75 A resolution. The domain has a modified, doubly wound alpha/beta fold in which one of the helices is replaced by an anti-parallel beta-hairpin. Previous biochemical and mutagenesis data, suggest that the methylester hydrolysis catalyzed by CheB proceeds through a mechanism involving a serine nucleophile. The methylesterase active site is tentatively identified as a cleft at the C-terminal edge of the beta-sheet containing residues Ser164, His190 and Asp286. The three-dimensional fold, and the arrangement of residues within the catalytic triad distinguishes the CheB methylesterase from any previously described serine protease or serine hydrolase.
About this Structure
1CHD is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB., West AH, Martinez-Hackert E, Stock AM, J Mol Biol. 1995 Jul 7;250(2):276-90. PMID:7608974
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