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"The structure of the E. coli recA protein monomer and polymer."

Story RM, Weber IT, Steitz TA



Published Feb. 23, 1992 in Nature volume 355 .

Pubmed ID: 1731246

Abstract:
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.


This publication refers to following REPAIRtoire entries:

Proteins


Last modification of this entry: Oct. 6, 2010

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