Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.2
Classification:HYDROLASE
Release Date:2014-11-12
Deposition Date:2014-08-28
Revision Date:2014-12-24#2015-02-04
Molecular Weight:82178.88
Macromolecule Type:Protein
Residue Count:710
Atom Site Count:4756
DOI:10.2210/pdb4wa8/pdb
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.
Resolution:2.2
Classification:HYDROLASE
Release Date:2014-11-12
Deposition Date:2014-08-28
Revision Date:2014-12-24#2015-02-04
Molecular Weight:82178.88
Macromolecule Type:Protein
Residue Count:710
Atom Site Count:4756
DOI:10.2210/pdb4wa8/pdb
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.
| Date made available | 2014 |
|---|---|
| Publisher | RCSB-PDB |