1zh2: Difference between revisions

Revision as of 23:49, 27 July 2008

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File:1zh2.png

Template:STRUCTURE 1zh2

Crystal Structure Of The Calcium-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpECrystal Structure Of The Calcium-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE

Template:ABSTRACT PUBMED 16322582

About this StructureAbout this Structure

1ZH2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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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-[[Image:1zh2.gif|left|200px]]
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 {{STRUCTURE_1zh2|  PDB=1zh2  |  SCENE=  }}
-'''Crystal Structure Of The Calcium-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE'''
+===Crystal Structure Of The Calcium-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16322582}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16322582 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16322582}}
 ==About this Structure==
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 [[Category: Transcription factor]]
 [[Category: Two-component system]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:36:55 2008''
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