Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair.
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.
Nakagawa
N
N
Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka, 560-0043, Japan.
Sugahara
M
M
Masui
R
R
Kato
R
R
Fukuyama
K
K
Kuramitsu
S
S
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D004265:DNA Helicases / Q000378:metabolism; D004260:DNA Repair; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D011487:Protein Conformation; D016963:Thermus thermophilus / Q000737:chemistry*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C058093:UvrB protein, E coli; D004247:DNA; D004265:DNA Helicases