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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...
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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
National Academy of Sciences
2011
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| Assuntos: | |
| Acceso en liña: | 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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