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 PubMed
The 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.
References
- ↑ Mondragon A, Subbiah S, Almo SC, Drottar M, Harrison SC. Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution. J Mol Biol. 1989 Jan 5;205(1):189-200. PMID:2926803
