2R6F

Crystal Structure of Bacillus stearothermophilus UvrA

Summary for 2R6F

• Entry DOI: 10.2210/pdb2r6f/pdb
• Descriptor: Excinuclease ABC subunit A, ADENOSINE-5'-DIPHOSPHATE, ZINC ION, ... (4 entities in total)
• Functional Keywords: uvra, nucleotide excision repair, dna repair, abc atpase, atp-binding cassette, dna damage, dna excision, dna-binding, excision nuclease, metal-binding, nucleotide-binding, sos response, hydrolase
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 2
• Total formula weight: 219670.46

Authors

Inuzuka, Y.,Pakotiprapha, D.,Bowman, B.R.,Jeruzalmi, D.,Verdine, G.L. (deposition date: 2007-09-05, release date: 2008-01-08, Last modification date: 2024-11-06)

Primary citation

Pakotiprapha, D.,Inuzuka, Y.,Bowman, B.R.,Moolenaar, G.F.,Goosen, N.,Jeruzalmi, D.,Verdine, G.L.
Crystal Structure of Bacillus stearothermophilus UvrA Provides Insight into ATP-Modulated Dimerization, UvrB Interaction, and DNA Binding.
Mol.Cell, 29:122-133, 2008

PubMed Abstract: The nucleotide excision repair pathway corrects many structurally unrelated DNA lesions. Damage recognition in bacteria is performed by UvrA, a member of the ABC ATPase superfamily whose functional form is a dimer with four nucleotide-binding domains (NBDs), two per protomer. In the 3.2 A structure of UvrA from Bacillus stearothermophilus, we observe that the nucleotide-binding sites are formed in an intramolecular fashion and are not at the dimer interface as is typically found in other ABC ATPases. UvrA also harbors two unique domains; we show that one of these is required for interaction with UvrB, its partner in lesion recognition. In addition, UvrA contains three zinc modules, the number and ligand sphere of which differ from previously published models. Structural analysis, biochemical experiments, surface electrostatics, and sequence conservation form the basis for models of ATP-modulated dimerization, UvrA-UvrB interaction, and DNA binding during the search for lesions.

PubMed: 18158267
DOI: 10.1016/j.molcel.2007.10.026

Experimental method

X-RAY DIFFRACTION (3.2 Å)