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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Detalles Bibliográficos
Autores principales: Uson, Maria Loressa, Carl, Ayala, Goldgur, Yehuda, Shuman, Stewart
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2018
Materias:
Nucleic Acid Enzymes
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5934675/
https://www.ncbi.nlm.nih.gov/pubmed/29635474
http://dx.doi.org/10.1093/nar/gky238

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5934675/
https://www.ncbi.nlm.nih.gov/pubmed/29635474
http://dx.doi.org/10.1093/nar/gky238

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