2NRZ

Crystal structure of the C-terminal half of UvrC bound to its catalytic divalent cation

Summary for 2NRZ

• Entry DOI: 10.2210/pdb2nrz/pdb
• Related: 1CYZ 2NRR 2NRT 2NRV 2NRW 2NRX
• Descriptor: UvrABC system protein C, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: uvrc, rnase h, endonuclase, helix hairpin helix, uvrabc, ner, divalent cation, manganese, hydrolase
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm : Q9WYA3
• Total number of polymer chains: 2
• Total formula weight: 50937.62

Authors

Karakas, E.,Truglio, J.J.,Kisker, C. (deposition date: 2006-11-02, release date: 2007-02-06, Last modification date: 2023-08-30)

Primary citation

Karakas, E.,Truglio, J.J.,Croteau, D.,Rhau, B.,Wang, L.,Van Houten, B.,Kisker, C.
Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.
Embo J., 26:613-622, 2007

PubMed Abstract: Removal and repair of DNA damage by the nucleotide excision repair pathway requires two sequential incision reactions, which are achieved by the endonuclease UvrC in eubacteria. Here, we describe the crystal structure of the C-terminal half of UvrC, which contains the catalytic domain responsible for 5' incision and a helix-hairpin-helix-domain that is implicated in DNA binding. Surprisingly, the 5' catalytic domain shares structural homology with RNase H despite the lack of sequence homology and contains an uncommon DDH triad. The structure also reveals two highly conserved patches on the surface of the protein, which are not related to the active site. Mutations of residues in one of these patches led to the inability of the enzyme to bind DNA and severely compromised both incision reactions. Based on our results, we suggest a model of how UvrC forms a productive protein-DNA complex to excise the damage from DNA.

PubMed: 17245438
DOI: 10.1038/sj.emboj.7601497

Experimental method

X-RAY DIFFRACTION (2 Å)