2D7D

Structural insights into the cryptic DNA dependent ATP-ase activity of UvrB

Summary for 2D7D

• Entry DOI: 10.2210/pdb2d7d/pdb
• Descriptor: 5'-D(P*TP*TP*T)-3', UvrABC system protein B, 40-mer from UvrABC system protein B, ... (5 entities in total)
• Functional Keywords: helicase, protein-dna-adp ternary complex, hydrolase-dna complex, hydrolase/dna
• Biological source: Bacillus subtilis; More
• Cellular location: Cytoplasm (By similarity): P37954 P37954
• Total number of polymer chains: 3
• Total formula weight: 82427.35

Authors

Barrett, T.E. (deposition date: 2005-11-18, release date: 2006-05-02, Last modification date: 2023-10-25)

Primary citation

Eryilmaz, J.,Ceschini, S.,Ryan, J.,Geddes, S.,Waters, T.R.,Barrett, T.E.
Structural insights into the cryptic DNA-dependent ATPase activity of UvrB
J.Mol.Biol., 357:62-72, 2006

PubMed Abstract: The UvrABC pathway is a ubiquitously occurring mechanism targeted towards the repair of bulky base damage. Key to this process is UvrB, a DNA-dependent limited helicase that acts as a lesion recognition element whilst part of a tracking complex involving UvrA, and as a DNA-binding platform required for the presentation of damage to UvrC for subsequent processing. We have been able to determine the structure of a ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP. This structure has highlighted the roles of key conserved residues in DNA binding distinct from those of the beta-hairpin, where most of the attention in previous studies has been focussed. We are also the first to report the structural basis underlying conformational re-modelling of the beta-hairpin that is absolutely required for DNA binding and how this event results in an ATPase primed for catalysis. Our data provide the first insights at the molecular level into the transformation of UvrB into an active helicase.

PubMed: 16426634
DOI: 10.1016/j.jmb.2005.12.059

Experimental method

X-RAY DIFFRACTION (2.1 Å)