6O8H

Crystal structure of UvrB mutant bound to duplex DNA

Summary for 6O8H

• Entry DOI: 10.2210/pdb6o8h/pdb
• Descriptor: UvrABC system protein B, DNA (5'-D(P*CP*CP*AP*TP*CP*GP*CP*GP*CP*TP*AP*CP*C)-3'), DNA (5'-D(P*AP*GP*CP*GP*CP*GP*AP*TP*GP*GP*AP*GP*A)-3'), ... (6 entities in total)
• Functional Keywords: dna repair, nucleotide excision repair, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Bacillus caldotenax; More
• Total number of polymer chains: 3
• Total formula weight: 78142.75

Authors

Lee, S.-J.,Verdine, G.L. (deposition date: 2019-03-10, release date: 2020-01-22, Last modification date: 2024-03-13)

Primary citation

Lee, S.J.,Sung, R.J.,Verdine, G.L.
Mechanism of DNA Lesion Homing and Recognition by the Uvr Nucleotide Excision Repair System.
Res, 2019:5641746-5641746, 2019

PubMed Abstract: Nucleotide excision repair (NER) is an essential DNA repair system distinguished from other such systems by its extraordinary versatility. NER removes a wide variety of structurally dissimilar lesions having only their bulkiness in common. NER can also repair several less bulky nucleobase lesions, such as 8-oxoguanine. Thus, how a single DNA repair system distinguishes such a diverse array of structurally divergent lesions from undamaged DNA has been one of the great unsolved mysteries in the field of genome maintenance. Here we employ a synthetic crystallography approach to obtain crystal structures of the pivotal NER enzyme UvrB in complex with duplex DNA, trapped at the stage of lesion-recognition. These structures coupled with biochemical studies suggest that UvrB integrates the ATPase-dependent helicase/translocase and lesion-recognition activities. Our work also conclusively establishes the identity of the lesion-containing strand and provides a compelling insight to how UvrB recognizes a diverse array of DNA lesions.

PubMed: 31549070
DOI: 10.34133/2019/5641746

Experimental method

X-RAY DIFFRACTION (2.39 Å)