1chd: Difference between revisions
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New page: left|200px<br /><applet load="1chd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1chd, resolution 1.75Å" /> '''CHEB METHYLESTERASE ... |
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[[Image:1chd.jpg|left|200px]]<br /><applet load="1chd" size=" | [[Image:1chd.jpg|left|200px]]<br /><applet load="1chd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1chd, resolution 1.75Å" /> | caption="1chd, resolution 1.75Å" /> | ||
'''CHEB METHYLESTERASE DOMAIN'''<br /> | '''CHEB METHYLESTERASE DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
Signaling activity of bacterial chemotaxis transmembrane receptors is | 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== | ==About this Structure== | ||
1CHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Active as [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] Full crystallographic information is available from [http:// | 1CHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Martinez-Hackert, E.]] | [[Category: Martinez-Hackert, E.]] | ||
[[Category: Stock, A | [[Category: Stock, A M.]] | ||
[[Category: West, A | [[Category: West, A H.]] | ||
[[Category: chemotaxis protein]] | [[Category: chemotaxis protein]] | ||
[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:11 2008'' | ||
