3V4R

Crystal structure of a UvrB dimer-DNA complex

Summary for 3V4R

• Entry DOI: 10.2210/pdb3v4r/pdb
• Descriptor: UvrABC system protein B, DNA: 5 -TACTGTTT-3, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: helicase motifs and a beta-hairpin, dna helicase, uvra, atp hydrolysis, hydrolase-dna complex, hydrolase/dna
• Biological source: Bacillus subtilis; More
• Cellular location: Cytoplasm (By similarity): P37954
• Total number of polymer chains: 4
• Total formula weight: 160207.64

Authors

Webster, M.P.J.,Jukes, R.,Barrett, T. (deposition date: 2011-12-15, release date: 2012-07-04, Last modification date: 2023-09-13)

Primary citation

Webster, M.P.,Jukes, R.,Zamfir, V.S.,Kay, C.W.,Bagneris, C.,Barrett, T.
Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes.
Nucleic Acids Res., 40:8743-8758, 2012

PubMed Abstract: UvrB has a central role in the highly conserved UvrABC pathway functioning not only as a damage recognition element but also as an essential component of the lesion tracking machinery. While it has been recently confirmed that the tracking assembly comprises a UvrA2B2 heterotetramer, the configurations of the damage engagement and UvrB-DNA handover complexes remain obscure. Here, we present the first crystal structure of a UvrB dimer whose biological significance has been verified using both chemical cross-linking and electron paramagnetic resonance spectroscopy. We demonstrate that this dimeric species stably associates with UvrA and forms a UvrA2B2-DNA complex. Our studies also illustrate how signals are transduced between the ATP and DNA binding sites to generate the helicase activity pivotal to handover and formation of the UvrB2-DNA complex, providing key insights into the configurations of these important repair intermediates.

PubMed: 22753105
DOI: 10.1093/nar/gks633

Experimental method

X-RAY DIFFRACTION (3.25 Å)