3FPN
Crystal structure of UvrA-UvrB interaction domains
Summary for 3FPN
Entry DOI | 10.2210/pdb3fpn/pdb |
Descriptor | Geobacillus stearothermophilus UvrA interaction domain, Geobacillus stearothermophilus UvrB interaction domain (3 entities in total) |
Functional Keywords | uvra, uvrb, nucleotide excision repair, dna repair, dna binding protein |
Biological source | Geobacillus stearothermophilus More |
Total number of polymer chains | 2 |
Total formula weight | 25710.46 |
Authors | Pakotiprapha, D.,Verdine, G.L.,Jeruzalmi, D. (deposition date: 2009-01-05, release date: 2009-03-24, Last modification date: 2023-09-06) |
Primary citation | Pakotiprapha, D.,Liu, Y.,Verdine, G.L.,Jeruzalmi, D. A Structural Model for the Damage-sensing Complex in Bacterial Nucleotide Excision Repair. J.Biol.Chem., 284:12837-12844, 2009 Cited by PubMed Abstract: Nucleotide excision repair is distinguished from other DNA repair pathways by its ability to process a wide range of structurally unrelated DNA lesions. In bacteria, damage recognition is achieved by the UvrA.UvrB ensemble. Here, we report the structure of the complex between the interaction domains of UvrA and UvrB. These domains are necessary and sufficient for full-length UvrA and UvrB to associate and thereby form the DNA damage-sensing complex of bacterial nucleotide excision repair. The crystal structure and accompanying biochemical analyses suggest a model for the complete damage-sensing complex. PubMed: 19287003DOI: 10.1074/jbc.M900571200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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