1cmc: Difference between revisions

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{{STRUCTURE_1cmc|  PDB=1cmc  |  SCENE=  }}  
{{STRUCTURE_1cmc|  PDB=1cmc  |  SCENE=  }}  


'''THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR'''
===THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR===




==Overview==
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The three-dimensional crystal structure of met repressor, in the presence or absence of bound corepressor (S-adenosylmethionine), shows a dimer of intertwined monomers, which do not have the helix-turn-helix motif characteristic of other bacterial repressor and activator structures. We propose that the interaction of met repressor with DNA occurs through either a pair of symmetry-related alpha-helices or a pair of beta-strands, and suggest a model for binding of several dimers to met operator regions.
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{{ABSTRACT_PUBMED_2677753}}


==About this Structure==
==About this Structure==
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[[Category: Somers, W S.]]
[[Category: Somers, W S.]]
[[Category: Dna-binding regulatory protein]]
[[Category: Dna-binding regulatory protein]]
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Revision as of 17:56, 30 June 2008

File:1cmc.png

Template:STRUCTURE 1cmc

THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR

Template:ABSTRACT PUBMED 2677753

About this Structure

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

Reference

Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor., Rafferty JB, Somers WS, Saint-Girons I, Phillips SE, Nature. 1989 Oct 26;341(6244):705-10. PMID:2677753

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