2FDC

Structural Basis of DNA Damage Recognition and Processing by UvrB: crystal structure of a UvrB/DNA complex

Summary for 2FDC

• Entry DOI: 10.2210/pdb2fdc/pdb
• Related: 1D9X 1D9Z 1QOJ 1T5L 1YD1
• Descriptor: 5'-D(P*CP*GP*GP*CP*TP*CP*CP*AP*TP*CP*TP*CP*TP*AP*CP*CP*GP*CP*AP*A)-3', UvrABC system protein B, N-[6-(ACETYLAMINO)HEXYL]-3',6'-DIHYDROXY-3-OXO-3H-SPIRO[2-BENZOFURAN-1,9'-XANTHENE]-6-CARBOXAMIDE (3 entities in total)
• Functional Keywords: protein-dna complex, uvrb, uvrc, uvrd, uvra, ner, nucleotide excision repair, dna repair, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Bacillus caldotenax
• Cellular location: Cytoplasm : P56981
• Total number of polymer chains: 4
• Total formula weight: 163720.33

Authors

Truglio, J.J.,Kisker, C. (deposition date: 2005-12-13, release date: 2006-03-14, Last modification date: 2024-02-14)

Primary citation

Truglio, J.J.,Karakas, E.,Rhau, B.,Wang, H.,DellaVecchia, M.J.,Van Houten, B.,Kisker, C.
Structural basis for DNA recognition and processing by UvrB.
Nat.Struct.Mol.Biol., 13:360-364, 2006

PubMed Abstract: DNA-damage recognition in the nucleotide excision repair (NER) cascade is a complex process, operating on a wide variety of damages. UvrB is the central component in prokaryotic NER, directly involved in DNA-damage recognition and guiding the DNA through repair synthesis. We report the first structure of a UvrB-double-stranded DNA complex, providing insights into the mechanism by which UvrB binds DNA, leading to formation of the preincision complex. One DNA strand, containing a 3' overhang, threads behind a beta-hairpin motif of UvrB, indicating that this motif inserts between the strands of the double helix, thereby locking down either the damaged or undamaged strand. The nucleotide directly behind the beta-hairpin is flipped out and inserted into a small, highly conserved pocket in UvrB.

PubMed: 16532007
DOI: 10.1038/nsmb1072

Experimental method

X-RAY DIFFRACTION (3.3 Å)