2or1
From Proteopedia
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'''RECOGNITION OF A DNA OPERATOR BY THE REPRESSOR OF PHAGE 434. A VIEW AT HIGH RESOLUTION''' | '''RECOGNITION OF A DNA OPERATOR BY THE REPRESSOR OF PHAGE 434. A VIEW AT HIGH RESOLUTION''' | ||
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[[Category: Ptashne, M.]] | [[Category: Ptashne, M.]] | ||
[[Category: Rodgers, D W.]] | [[Category: Rodgers, D W.]] | ||
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Revision as of 08:29, 4 May 2008
RECOGNITION OF A DNA OPERATOR BY THE REPRESSOR OF PHAGE 434. A VIEW AT HIGH RESOLUTION
Overview
The repressors of temperate bacteriophages such as 434 and lambda control transcription by binding to a set of DNA operator sites. The different affinity of repressor for each of these sites ensures efficient regulation. High-resolution x-ray crystallography was used to study the DNA-binding domain of phage 434 repressor in complex with a synthetic DNA operator. The structure shows recognition of the operator by direct interactions with base pairs in the major groove, combined with the sequence-dependent ability of DNA to adopt the required conformation on binding repressor. In particular, a network of three-centered bifurcated hydrogen bonds among base pairs in the operator helps explain why 434 repressor prefers certain sites over others. These bonds, which stabilize the conformation of the bound DNA, can form only with certain sequences.
About this Structure
2OR1 is a Single protein structure of sequence from Phage 434. Full crystallographic information is available from OCA.
Reference
Recognition of a DNA operator by the repressor of phage 434: a view at high resolution., Aggarwal AK, Rodgers DW, Drottar M, Ptashne M, Harrison SC, Science. 1988 Nov 11;242(4880):899-907. PMID:3187531 Page seeded by OCA on Sun May 4 11:29:58 2008