Structure and specificity of FEN-1 from Methanopyrus kandleri
- Univ. of Arizona, Tucson, AZ (United States). Dept. of Chemistry and Biochemistry
- SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
ABSTRACT DNA repair is fundamental to genome stability and is found in all three domains of life. However many archaeal species, such as Methanopyrus kandleri , contain only a subset of the eukaryotic nucleotide excision repair (NER) homologs, and those present often contain significant differences compared to their eukaryotic homologs. To clarify the role of the NER XPG‐like protein Mk0566 from M. kandleri , its biochemical activity and three‐dimensional structure were investigated. Both were found to be more similar to human FEN‐1 than human XPG, suggesting a biological role in replication and long‐patch base excision repair rather than in NER. Proteins 2015; 83:188–194. © 2014 Wiley Periodicals, Inc.
- Research Organization:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)
- Grant/Contract Number:
- AC02-76SF00515; P41GM103393; S10OD013237
- OSTI ID:
- 1291006
- Alternate ID(s):
- OSTI ID: 1400880
- Journal Information:
- Proteins, Vol. 83, Issue 1; ISSN 0887-3585
- Publisher:
- WileyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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