2pl1: Difference between revisions

Revision as of 09:53, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2pl1.png

2pl1, resolution 1.90Å ()

Ligands:

, ,

Non-Standard Residues:

Gene:

phoP (Escherichia coli)

Related:

2pkx

Structural annotation:
Resources:	InterPro : Ipr011006, Ipr001867, Ipr001789 Pfam : PF00072 UniProt : P23836

Functional annotation:
Cellular component:	cytoplasm
Biological process:	regulation of transcription, DNA-dependent transcription two-component signal transduction system (phosphorelay)
Molecular function:	DNA binding two-component response regulator activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

Berrylium Fluoride activated receiver domain of E.coli PhoPBerrylium Fluoride activated receiver domain of E.coli PhoP

Template:ABSTRACT PUBMED 17545283

About this StructureAbout this Structure

2PL1 is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 2eub. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride., Bachhawat P, Stock AM, J Bacteriol. 2007 Aug;189(16):5987-95. Epub 2007 Jun 1. PMID:17545283

Page seeded by OCA on Mon Jul 28 09:53:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Berrylium Fluoride activated receiver domain of E.coli PhoP'''
+===Berrylium Fluoride activated receiver domain of E.coli PhoP===
-==Overview==
+<!--
-The response regulator PhoP is part of the PhoQ/PhoP two-component system involved in responses to depletion of extracellular Mg(2+). Here, we report the crystal structures of the receiver domain of Escherichia coli PhoP determined in the absence and presence of the phosphoryl analog beryllofluoride. In the presence of beryllofluoride, the active receiver domain forms a twofold symmetric dimer similar to that seen in structures of other regulatory domains from the OmpR/PhoB family, providing further evidence that members of this family utilize a common mode of dimerization in the active state. In the absence of activating agents, the PhoP receiver domain crystallizes with a similar structure, consistent with the previous observation that high concentrations can promote an active state of PhoP independent of phosphorylation.
+The line below this paragraph, {{ABSTRACT_PUBMED_17545283}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17545283 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17545283}}
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 [[Category: Transcription factor]]
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