1cmc
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(New page: 200px<br /><applet load="1cmc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmc, resolution 1.8Å" /> '''THREE DIMENSIONAL CRY...)
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Revision as of 10:27, 20 November 2007
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THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR
Overview
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.
About this Structure
1CMC is a Single protein structure of sequence from Escherichia coli with MG and SAM as ligands. 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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