1D2M

UVRB PROTEIN OF THERMUS THERMOPHILUS HB8; A NUCLEOTIDE EXCISION REPAIR ENZYME

Summary for 1D2M

• Entry DOI: 10.2210/pdb1d2m/pdb
• Descriptor: EXCINUCLEASE ABC SUBUNIT B, octyl beta-D-glucopyranoside, SULFATE ION, ... (4 entities in total)
• Functional Keywords: multidomain protein, riken structural genomics/proteomics initiative, rsgi, structural genomics, hydrolase
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: Q56243
• Total number of polymer chains: 1
• Total formula weight: 77239.29

Authors

Nakagawa, N.,Sugahara, M.,Masui, R.,Kato, R.,Fukuyama, K.,Kuramitsu, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 1999-09-25, release date: 2000-03-22, Last modification date: 2024-02-07)

Primary citation

Nakagawa, N.,Sugahara, M.,Masui, R.,Kato, R.,Fukuyama, K.,Kuramitsu, S.
Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair.
J.Biochem.(Tokyo), 126:986-990, 1999

PubMed 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 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.

PubMed: 10578047

Experimental method

X-RAY DIFFRACTION (1.9 Å)