THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMERTHE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER

Structural highlights

2reb is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

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 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 Also

References

  1. Story RM, Weber IT, Steitz TA. The structure of the E. coli recA protein monomer and polymer. Nature. 1992 Jan 23;355(6358):318-25. PMID:1731246 doi:http://dx.doi.org/10.1038/355318a0

2reb, resolution 2.30Å

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