User:Elizabeth R. Haglin/Sandbox 1

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== Structure ==
== Structure ==
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[[Image:CheA_domains.png|250px|right|tumb|CheA Domains <ref>PMID: 22494339</ref>]]
The isolated CheA kinase exists as a homodimer of 71-kDa subunits, each of which catalyzes ATP-dependent ''trans''-phosphorylation of a histidine. A CheA monomer contains 5 domains (named P1-P5 from N- to C-terminus) connected by highly dynamic linkers of various lengths. Each domain has a distinct and important function.
The isolated CheA kinase exists as a homodimer of 71-kDa subunits, each of which catalyzes ATP-dependent ''trans''-phosphorylation of a histidine. A CheA monomer contains 5 domains (named P1-P5 from N- to C-terminus) connected by highly dynamic linkers of various lengths. Each domain has a distinct and important function.
*P1: a histidine phosphotransfer domain (HPt) acting as an intermediate for phosphate transfer from ATP to CheY
*P1: a histidine phosphotransfer domain (HPt) acting as an intermediate for phosphate transfer from ATP to CheY

Revision as of 19:43, 12 December 2012

Structure of CheA (PDB entry 1b3q)

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Elizabeth R. Haglin

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