Crystal Structure of Thermus thermophilus HB8 UvrB Protein, a Key Enzyme of Nucleotide Excision Repair

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In the nucleotide excision repair system, UvrB plays a central role in damage recognition and DNA incision by interacting with UvrA and UvrC. We have determined the crystal structure of Thermus thermophilus HB8 UvrB at 1.9 Å resolution. UvrB comprises four domains, two of which have an α/β structure resembling the core domains of DNA and RNA helicases. Additionally, UvrB has an α-helical domain and a domain consisting of antiparallel β-sheets (β-domain). The sequence similarity suggests that the β-domain interacts with UvrA. Based on the distribution of the conserved regions and the structure of the PcrA-DNA complex, a model for the UvrB-DNA complex is proposed.