3ux8
Crystal structure of UvrACrystal structure of UvrA
Structural highlights
Function[E8SW61_GEOS2] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (By similarity).[HAMAP-Rule:MF_00205] Publication Abstract from PubMedNucleotide excision repair (NER) is used by all organisms to eliminate DNA lesions. We determined the structure of the Geobacillus stearothermophilus UvrA-UvrB complex, the damage-sensor in bacterial NER and a new structure of UvrA. We observe that the DNA binding surface of UvrA, previously found in an open shape that binds damaged DNA, also exists in a closed groove shape compatible with native DNA only. The sensor contains two UvrB molecules that flank the UvrA dimer along the predicted path for DNA, ~80 A from the lesion. We show that the conserved signature domain II of UvrA mediates a nexus of contacts among UvrA, UvrB and DNA. Further, in our new structure of UvrA, this domain adopts an altered conformation while an adjacent nucleotide binding site is vacant. Our findings raise unanticipated questions about NER and also suggest a revised picture of its early stages. Structure and mechanism of the UvrA-UvrB DNA damage sensor.,Pakotiprapha D, Samuels M, Shen K, Hu JH, Jeruzalmi D Nat Struct Mol Biol. 2012 Feb 5;19(3):291-8. doi: 10.1038/nsmb.2240. PMID:22307053[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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