3UWX
Crystal structure of UvrA-UvrB complex
Summary for 3UWX
| Entry DOI | 10.2210/pdb3uwx/pdb |
| Descriptor | Excinuclease ABC, A subunit, UvrABC system protein B, ZINC ION (3 entities in total) |
| Functional Keywords | uvra, uvrb, nucleotide excision repair, dna repair, abc atpase, atp binding, dna binding, dna binding protein |
| Biological source | Geobacillus More |
| Cellular location | Cytoplasm (By similarity): E8SW61 E8SW62 |
| Total number of polymer chains | 2 |
| Total formula weight | 186455.69 |
| Authors | Pakotiprapha, D.,Jeruzalmi, D. (deposition date: 2011-12-03, release date: 2012-02-08, Last modification date: 2024-02-28) |
| Primary citation | Pakotiprapha, D.,Samuels, M.,Shen, K.,Hu, J.H.,Jeruzalmi, D. Structure and mechanism of the UvrA-UvrB DNA damage sensor. Nat.Struct.Mol.Biol., 19:291-298, 2012 Cited by PubMed Abstract: Nucleotide 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 Å 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. PubMed: 22307053DOI: 10.1038/nsmb.2240 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.398 Å) |
Structure validation
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