Publication Abstract from PubMed
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 A resolution. UvrB comprises four domains, two of which have an alpha/beta structure resembling the core domains of DNA and RNA helicases. Additionally, UvrB has an alpha-helical domain and a domain consisting of antiparallel beta-sheets (beta-domain). The sequence similarity suggests that the beta-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.
Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair.,Nakagawa N, Sugahara M, Masui R, Kato R, Fukuyama K, Kuramitsu S J Biochem. 1999 Dec;126(6):986-90. PMID:10578047[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
