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Article

Crystal structures of lambda exonuclease in complex with DNA suggest an electrostatic ratchet mechanism for processivity.

Proceedings of the National Academy of Sciences of the United States of America - 19 Jul 2011

Zhang Jinjin, McCabe Kimberly A, Bell Charles E

Abstract excerpt

The λ exonuclease is an ATP-independent enzyme that binds to dsDNA ends and processively digests the 5'-ended strand to form 5' mononucleotides and a long 3' overhang. The crystal structure of λ exonuclease revealed a toroidal homotrimer with a central funnel-shaped channel for tracking along the DNA, and a mechanism for processivity based on topological linkage of the trimer to the DNA was proposed. Here, we...

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Identifiers

PMID: 21730170
DOI: 10.1073/pnas.1103467108
PMCID: PMC3141983

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