2or1: Difference between revisions

Revision as of 16:11, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2or1.png

Template:STRUCTURE 2or1

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

Template:ABSTRACT PUBMED 3187531

About this StructureAbout this Structure

2OR1 is a Single protein structure of sequence from Phage 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

Page seeded by OCA on Mon Jul 28 16:11:06 2008

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OCA

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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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_3187531}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 3187531 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_3187531}}
 ==About this Structure==
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 [[Category: Double helix]]
 [[Category: Protein-dna complex]]
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