1hxd

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[[Image:1hxd.gif|left|200px]]
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{{STRUCTURE_1hxd| PDB=1hxd | SCENE= }}
{{STRUCTURE_1hxd| PDB=1hxd | SCENE= }}
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'''CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN'''
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===CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN===
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==Overview==
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The Escherichia coli biotin repressor binds to the biotin operator to repress transcription of the biotin biosynthetic operon. In this work, a structure determined by x-ray crystallography of a complex of the repressor bound to biotin, which also functions as an activator of DNA binding by the biotin repressor (BirA), is described. In contrast to the monomeric aporepressor, the complex is dimeric with an interface composed in part of an extended beta-sheet. Model building, coupled with biochemical data, suggests that this is the dimeric form of BirA that binds DNA. Segments of three surface loops that are disordered in the aporepressor structure are located in the interface region of the dimer and exhibit greater order than was observed in the aporepressor structure. The results suggest that the corepressor of BirA causes a disorder-to-order transition that is a prerequisite to repressor dimerization and DNA binding.
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(as it appears on PubMed at http://www.pubmed.gov), where 11353844 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11353844}}
==About this Structure==
==About this Structure==
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[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Repressor]]
[[Category: Repressor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:04:07 2008''

Revision as of 07:04, 1 July 2008

Template:STRUCTURE 1hxd

CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN

Template:ABSTRACT PUBMED 11353844

About this Structure

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

Reference

Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator., Weaver LH, Kwon K, Beckett D, Matthews BW, Proc Natl Acad Sci U S A. 2001 May 22;98(11):6045-50. Epub 2001 May 15. PMID:11353844

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