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-Reference-Cited by-同舟云学术

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

Published:2018-04-09 Issue:8 Volume:46 Page:4164-4175
ISSN:0305-1048
Container-title:Nucleic Acids Research
language:en
Short-container-title:

Author:

Uson Maria Loressa¹,Carl Ayala¹,Goldgur Yehuda²,Shuman Stewart¹

Affiliation:

1. Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA

2. Structural Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA

Funder

National Institutes of Health

National Cancer Institute

Department of Energy

Publisher

Oxford University Press (OUP)

Subject

Genetics

Link

http://academic.oup.com/nar/article-pdf/46/8/4164/24783340/gky238.pdf

Reference40 articles.

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2. Substrate recognition and catalysis by flap endonucleases and related enzymes;Tomlinson;Biochem. Soc. Trans.,2010

3. Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases;Lyamichev;Science,1993

4. Biochemical and mutational studies of the 5′-3′ exonuclease of DNA polymerase I of Escherichia coli;Xu;J. Mol. Biol.,1997

5. Comparison of the 5′ nuclease activities of Taq DNA polymerase and its isolated nuclease domain;Lyamichev;Proc. Natl. Acad. Sci. U.S.A.,1999

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