1r69 | pdb_00001r69
From Proteopedia
STRUCTURE OF THE AMINO-TERMINAL DOMAIN OF PHAGE 434 REPRESSOR AT 2.0 ANGSTROMS RESOLUTION
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Structural highlights
Function[RPC1_BP434] Binds to two sets of three contiguous operator sites in the phage genome. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the amino-terminal domain of phage 434 repressor has been solved using molecular replacement methods and refined to an R-factor of 19.3% against data to 2.0 A resolution. The protein comprises five short alpha-helices. Two of these form a helix-turn-helix motif, very similar to those found in related proteins. The protein is remarkably similar to the Cro protein from the same phage. Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution.,Mondragon A, Subbiah S, Almo SC, Drottar M, Harrison SC J Mol Biol. 1989 Jan 5;205(1):189-200. PMID:2926803[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences | ||||||||||||||||
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