2iyn: Difference between revisions

Revision as of 15:02, 27 July 2008

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File:2iyn.png

Template:STRUCTURE 2iyn

THE CO-FACTOR-INDUCED PRE-ACTIVE CONFORMATION IN PHOBTHE CO-FACTOR-INDUCED PRE-ACTIVE CONFORMATION IN PHOB

Template:ABSTRACT PUBMED 16929106

About this StructureAbout this Structure

2IYN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

The cofactor-induced pre-active conformation in PhoB., Sola M, Drew DL, Blanco AG, Gomis-Ruth FX, Coll M, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1046-57. Epub 2006, Aug 19. PMID:16929106

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

OCA

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 {{STRUCTURE_2iyn|  PDB=2iyn  |  SCENE=  }}
-'''THE CO-FACTOR-INDUCED PRE-ACTIVE CONFORMATION IN PHOB'''
+===THE CO-FACTOR-INDUCED PRE-ACTIVE CONFORMATION IN PHOB===
-==Overview==
+<!--
-PhoB is an Escherichia coli transcription factor from a two-component signal transduction system that is sensitive to limiting environmental phosphate conditions. It consists of an N-terminal receiver domain (RD) and a C-terminal DNA-binding domain. The protein is activated upon phosphorylation at the RD, an event that depends on Mg(2+) binding. The structure of PhoB RD in complex with Mg(2+) is presented, which shows three protomers in the asymmetric unit that interact across two different surfaces. One association is symmetric and has been described as a non-active dimerization contact; the other involves the alpha4-beta5-alpha5 interface and recalls the contact found in activated PhoB. However, here this last interaction is not perfectly symmetric and helix alpha4, which in the activated molecule undergoes a helical shift, becomes strongly destabilized in one of the interacting monomers. All protomers bind the cation in a similar manner but, interestingly, at the prospective binding site for the phosphate moiety the side chains of either Glu88 (in helix alpha4) or Trp54 alternate and interact with active-site atoms. When Glu88 is inside the cavity, helix alpha4 is arranged similarly to the unliganded wild-type structure. However, if Trp54 is present, the helix loses its contacts with the active-site cavity and vanishes. Accordingly, the presence of Trp54 in the active site induces a flexible state in helix alpha4, potentially allowing a helical shift that phosphorylation would eventually stabilize.
+The line below this paragraph, {{ABSTRACT_PUBMED_16929106}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16929106 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16929106}}
 ==About this Structure==
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 [[Category: Transport]]
 [[Category: Two-component regulatory system]]
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