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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.

A structural model for the damage-sensing complex in bacterial nucleotide excision repair., Pakotiprapha D, Liu Y, Verdine GL, Jeruzalmi D, J Biol Chem. 2009 May 8;284(19):12837-44. Epub 2009 Mar 13. PMID:19287003

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Categories: Geobacillus stearothermophilus | Jeruzalmi, D. | Pakotiprapha, D. | Verdine, G L. | Dna binding protein | Dna repair | Nucleotide excision repair | Uvra | Uvrb