2iyn

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Revision as of 20:42, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2iyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iyn, resolution 2.08Å" /> '''THE CO-FACTOR-INDUC...)
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File:2iyn.gif


2iyn, resolution 2.08Å

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

OverviewOverview

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 ... [(full description)]

About this StructureAbout this Structure

2IYN is a [Single protein] structure of sequence from [Escherichia coli] with MG as [ligand]. 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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