1a2o
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(New page: 200px<br /> <applet load="1a2o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a2o, resolution 2.4Å" /> '''STRUCTURAL BASIS FOR...)
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Revision as of 16:47, 29 October 2007
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STRUCTURAL BASIS FOR METHYLESTERASE CHEB REGULATION BY A PHOSPHORYLATION-ACTIVATED DOMAIN
Overview
We report the x-ray crystal structure of the methylesterase CheB, a, phosphorylation-activated response regulator involved in reversible, modification of bacterial chemotaxis receptors. Methylesterase CheB and, methyltransferase CheR modulate signaling output of the chemotaxis, receptors by controlling the level of receptor methylation. The structure, of CheB, which consists of an N-terminal regulatory domain and a, C-terminal catalytic domain joined by a linker, was solved by molecular, replacement methods using independent search models for the two domains., In unphosphorylated CheB, the N-terminal domain packs against the active, site of the C-terminal domain and thus inhibits methylesterase activity by, directly restricting access to the active site. We propose that, phosphorylation ... [(full description)]
About this Structure
1A2O is a [Single protein] structure of sequence from [Salmonella typhimurium]. Active as [[1]], with EC number [3.1.1.61]. Full crystallographic information is available from [OCA].
Reference
Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain., Djordjevic S, Goudreau PN, Xu Q, Stock AM, West AH, Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1381-6. PMID:9465023
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