1chd: Difference between revisions

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[[Image:1chd.jpg|left|200px]]
{{Seed}}
[[Image:1chd.png|left|200px]]


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{{STRUCTURE_1chd|  PDB=1chd  |  SCENE=  }}  
{{STRUCTURE_1chd|  PDB=1chd  |  SCENE=  }}  


'''CHEB METHYLESTERASE DOMAIN'''
===CHEB METHYLESTERASE DOMAIN===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_7608974}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_7608974}}


==About this Structure==
==About this Structure==
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[[Category: Chemotaxis protein]]
[[Category: Chemotaxis protein]]
[[Category: Serine hydrolase]]
[[Category: Serine hydrolase]]
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