1zh4

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(New page: 200px<br /><applet load="1zh4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zh4, resolution 2.20&Aring;" /> '''Crystal Structure Of...)
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Revision as of 05:19, 21 November 2007


1zh4, resolution 2.20Å

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Crystal Structure Of The Mg+2/BeF3-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE

Overview

Bacterial response regulators are key regulatory proteins that function as, the final elements of so-called two-component signaling systems. The, activities of response regulators in vivo are modulated by phosphorylation, that results from interactions between the response regulator and its, cognate histidine protein kinase. The level of response regulator, phosphorylation, which is regulated by intra-or extracellular signals, sensed by the histidine protein kinase, ultimately determines the output, response that is initiated or carried out by the response regulator. We, have recently hypothesized that in the OmpR/PhoB subfamily of response, regulator transcription factors, this activation involves a common, mechanism of dimerization using a set of highly conserved residues in the, alpha4-beta5-alpha5 face. Here we report the X-ray crystal structures of, the regulatory domains of response regulators TorR (1.8 A), Ca(2+)-bound, KdpE (2.0 A), and Mg(2+)/BeF(3)(-)-bound KdpE (2.2 A), both members of the, OmpR/ PhoB subfamily from Escherichia coli. Both regulatory domains form, symmetric dimers in the asymmetric unit that involve the, alpha4-beta5-alpha5 face. As observed previously in other OmpR/PhoB, response regulators, the dimer interfaces are mediated by highly conserved, residues within this subfamily. These results provide further evidence, that most all response regulators of the OmpR/ PhoB subfamily share a, common mechanism of activation by dimerization.

About this Structure

1ZH4 is a Single protein structure of sequence from Escherichia coli with MG and BEF as ligands. Full crystallographic information is available from OCA.

Reference

A common dimerization interface in bacterial response regulators KdpE and TorR., Toro-Roman A, Wu T, Stock AM, Protein Sci. 2005 Dec;14(12):3077-88. PMID:16322582

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