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

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 DN...

詳細記述

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書誌詳細
主要な著者: Zhang, Jinjin, McCabe, Kimberly A., Bell, Charles E.
フォーマット: Artigo
言語:Inglês
出版事項: National Academy of Sciences 2011
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC3141983/
https://ncbi.nlm.nih.gov/pubmed/21730170
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1103467108
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