3FPN: Crystal structure of UvrA-UvrB interaction domains

Citation:
Abstract
Nucleotide excision repair is distinguished from other DNA repair pathways by its ability to process a wide range of structurally unrelated DNA lesions. In bacteria, damage recognition is achieved by the UvrA.UvrB ensemble. Here, we report the structure of the complex between the interaction domains of UvrA and UvrB. These domains are necessary and sufficient for full-length UvrA and UvrB to associate and thereby form the DNA damage-sensing complex of bacterial nucleotide excision repair. The crystal structure and accompanying biochemical analyses suggest a model for the complete damage-sensing complex.
PDB ID: 3FPNDownload
MMDB ID: 70400
PDB Deposition Date: 2009/1/5
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3FPN: dimeric; determined by author
Molecular Components in 3FPN
Label Count Molecule
Proteins (2 molecules)
1
Geobacillus Stearothermophilus Uvra Interaction Domain
Molecule annotation
1
Geobacillus Stearothermophilus Uvrb Interaction Domain
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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