Crystal Structure of Thermus thermophilus HB8 UvrB Protein, a Key Enzyme of Nucleotide Excision Repair
- 1 December 1999
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 126 (6) , 986-990
- https://doi.org/10.1093/oxfordjournals.jbchem.a022566
Abstract
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 a/P structure resembling the core domains of DNA and RNA helicases. Additionally, UvrB has an a-helical domain and a domain consisting of antipar-allel 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.Keywords
This publication has 0 references indexed in Scilit: