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
- Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA
- Structural Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA
- Sponsoring Organization:
- USDOE
- Grant/Contract Number:
- AC02-06CH11357
- OSTI ID:
- 1432392
- Journal Information:
- Nucleic Acids Research, Journal Name: Nucleic Acids Research Vol. 46 Journal Issue: 8; ISSN 0305-1048
- Publisher:
- Oxford University PressCopyright Statement
- Country of Publication:
- United Kingdom
- Language:
- English
Cited by: 5 works
Citation information provided by
Web of Science
Web of Science
Similar Records
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
Crystallization and preliminary crystallographic analysis of PimA, an essential mannosyltransferase from Mycobacterium smegmatis
Crystal structure of type I 3-dehydroquinate dehydratase of Aquifex aeolicus suggests closing of active site flap is not essential for enzyme action
Journal Article
·
Mon Apr 09 00:00:00 EDT 2018
· Nucleic Acids Research
·
OSTI ID:1432392
+1 more
Crystallization and preliminary crystallographic analysis of PimA, an essential mannosyltransferase from Mycobacterium smegmatis
Journal Article
·
Sun May 01 00:00:00 EDT 2005
· Acta Crystallographica. Section F
·
OSTI ID:1432392
+1 more
Crystal structure of type I 3-dehydroquinate dehydratase of Aquifex aeolicus suggests closing of active site flap is not essential for enzyme action
Journal Article
·
Fri Mar 01 00:00:00 EST 2013
· Biochemical and Biophysical Research Communications
·
OSTI ID:1432392
+3 more