6N9L
Crystal structure of T. maritima UvrA d117-399 with ADP
Summary for 6N9L
| Entry DOI | 10.2210/pdb6n9l/pdb |
| Descriptor | UvrABC system protein A, ZINC ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | dna binding protein, uvra, nucleotide excision repair, ner, adp, hydrolase, dna damage repair |
| Biological source | Thermotoga maritima More |
| Total number of polymer chains | 1 |
| Total formula weight | 72249.51 |
| Authors | Hartley, S.,Case, B.,Osuga, M.,Hingorani, M.M.,Jeruzalmi, D. (deposition date: 2018-12-03, release date: 2019-05-01, Last modification date: 2023-10-11) |
| Primary citation | Case, B.C.,Hartley, S.,Osuga, M.,Jeruzalmi, D.,Hingorani, M.M. The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair. Nucleic Acids Res., 47:4136-4152, 2019 Cited by PubMed Abstract: The UvrA2 dimer finds lesions in DNA and initiates nucleotide excision repair. Each UvrA monomer contains two essential ATPase sites: proximal (P) and distal (D). The manner whereby their activities enable UvrA2 damage sensing and response remains to be clarified. We report three key findings from the first pre-steady state kinetic analysis of each site. Absent DNA, a P2ATP-D2ADP species accumulates when the low-affinity proximal sites bind ATP and enable rapid ATP hydrolysis and phosphate release by the high-affinity distal sites, and ADP release limits catalytic turnover. Native DNA stimulates ATP hydrolysis by all four sites, causing UvrA2 to transition through a different species, P2ADP-D2ADP. Lesion-containing DNA changes the mechanism again, suppressing ATP hydrolysis by the proximal sites while distal sites cycle through hydrolysis and ADP release, to populate proximal ATP-bound species, P2ATP-Dempty and P2ATP-D2ATP. Thus, damaged and native DNA trigger distinct ATPase site activities, which could explain why UvrA2 forms stable complexes with UvrB on damaged DNA compared with weaker, more dynamic complexes on native DNA. Such specific coupling between the DNA substrate and the ATPase mechanism of each site provides new insights into how UvrA2 utilizes ATP for lesion search, recognition and repair. PubMed: 30892613DOI: 10.1093/nar/gkz180 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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