2r6f
Crystal Structure of Bacillus stearothermophilus UvrA
|
OverviewOverview
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.
About this StructureAbout this Structure
2R6F is a Single protein structure of sequence from Geobacillus stearothermophilus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal Structure of Bacillus stearothermophilus UvrA Provides Insight into ATP-Modulated Dimerization, UvrB Interaction, and DNA Binding., Pakotiprapha D, Inuzuka Y, Bowman BR, Moolenaar GF, Goosen N, Jeruzalmi D, Verdine GL, Mol Cell. 2008 Jan 18;29(1):122-33. Epub 2007 Dec 27. PMID:18158267
Page seeded by OCA on Wed Jan 23 11:15:49 2008