3v4r | pdb_00003v4r

Crystal structure of a UvrB dimer-DNA complex

spinqualitylabelsall models 3v4r, resolution 3.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3v4r is a 4 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP Gene: BSU35170, dinA, uvr, uvrB ("Bacillus globigii" Migula 1900) Activity: Type III site-specific deoxyribonuclease, with EC number 3.1.21.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [UVRB_BACSU] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage (By similarity). Publication Abstract from PubMed 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 UvrA(2)B(2) 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 UvrA(2)B(2)-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 UvrB(2)-DNA complex, providing key insights into the configurations of these important repair intermediates. Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes.,Webster MP, Jukes R, Zamfir VS, Kay CW, Bagneris C, Barrett T Nucleic Acids Res. 2012 Sep 1;40(17):8743-8758. Epub 2012 Jun 30. PMID:22753105 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also UvrABC

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