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1d2m

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1d2m, resolution 1.90Å ()
Ligands: ,
Domains: PRK05298, UVR, HELICc, DEXHc
Resources: FirstGlance, OCA, PDBsum, RCSB, TOPSAN
Coordinates: save as pdb, mmCIF, xml



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

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1D2M is a 1 chain structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

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

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