1kgs
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(New page: 200px<br /><applet load="1kgs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kgs, resolution 1.50Å" /> '''Crystal Structure at...)
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Revision as of 23:12, 24 November 2007
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Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima
Overview
Two-component systems, the predominant signal transduction strategy used, by prokaryotes, involve phosphorelay from a sensor histidine kinase (HK), to an intracellular response regulator protein (RR) that typically acts as, a transcription regulator. RRs are modular proteins, usually composed of a, conserved regulatory domain, which functions as a, phosphorylation-activated switch, and an attached DNA binding effector, domain. The crystal structure of a Thermotoga maritima transcription, factor, DrrD, has been determined at 1.5 A resolution, providing the first, structural information for a full-length member of the OmpR/PhoB subfamily, of RRs. A small interdomain interface occurs between alpha 5 of the, regulatory domain and an antiparallel sheet of the effector domain. The, lack of an extensive interface in the unphosphorylated protein, distinguishes DrrD from other structurally characterized multidomain RRs, and suggests a different mode of interdomain regulation.
About this Structure
1KGS is a Single protein structure of sequence from Thermotoga maritima with SCN as ligand. Full crystallographic information is available from OCA.
Reference
Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima., Buckler DR, Zhou Y, Stock AM, Structure. 2002 Feb;10(2):153-64. PMID:11839301
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