2or1

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Revision as of 14:08, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2or1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2or1, resolution 2.500Å" /> '''RECOGNITION OF A DN...)
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File:2or1.jpg


2or1, resolution 2.500Å

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RECOGNITION OF A DNA OPERATOR BY THE REPRESSOR OF PHAGE 434. A VIEW AT HIGH RESOLUTION

OverviewOverview

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 StructureAbout this Structure

2OR1 is a Single protein structure of sequence from Bacteriophage 434. Full crystallographic information is available from OCA.

ReferenceReference

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

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