1d2m

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Image:1d2m.jpg

1d2m, resolution 1.90Å

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

Overview

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.

About this Structure

1D2M is a Single protein structure of sequence from Thermus thermophilus with BOG and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

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 (Tokyo). 1999 Dec;126(6):986-90. PMID:10578047

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