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Crystal structure and mutational analysis of Mycobacterium smegmatis FenA highlight active site amino acids and three metal ions essential for flap endonuclease and 5′ exonuclease activities

Mycobacterium smegmatis FenA is a nucleic acid phosphodiesterase with flap endonuclease and 5′ exonuclease activities. The 1.8 Å crystal structure of FenA reported here highlights as its closest homologs bacterial FEN-family enzymes ExoIX, the Pol1 exonuclease domain and phage T5 Fen. Mycobacterial...

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Detalhes bibliográficos
Publicado no:Nucleic Acids Res
Main Authors: Uson, Maria Loressa, Carl, Ayala, Goldgur, Yehuda, Shuman, Stewart
Formato: Artigo
Idioma:Inglês
Publicado em: Oxford University Press 2018
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC5934675/
https://ncbi.nlm.nih.gov/pubmed/29635474
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/nar/gky238
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