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THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMERTHE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER
Structural highlights
Evolutionary ConservationCheck, 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 recA protein from Escherichia coli at 2.3-A resolution reveals a major domain that binds ADP and probably single- and double-stranded DNA. Two smaller subdomains at the N and C termini protrude from the protein and respectively stabilize a 6(1) helical polymer of protein subunits and interpolymer bundles. This polymer structure closely resembles that of recA/DNA filaments determined by electron microscopy. Mutations in recA protein that enhance coprotease, DNA-binding and/or strand-exchange activity can be explained if the interpolymer interactions in the crystal reflect a regulatory mechanism in vivo. The structure of the E. coli recA protein monomer and polymer.,Story RM, Weber IT, Steitz TA Nature. 1992 Jan 23;355(6358):318-25. PMID:1731246[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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