2d7d
From Proteopedia
Structural insights into the cryptic DNA dependent ATP-ase activity of UvrB
Overview
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.
About this Structure
2D7D is a Protein complex structure of sequences from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structural insights into the cryptic DNA-dependent ATPase activity of UvrB., Eryilmaz J, Ceschini S, Ryan J, Geddes S, Waters TR, Barrett TE, J Mol Biol. 2006 Mar 17;357(1):62-72. Epub 2006 Jan 6. PMID:16426634 Page seeded by OCA on Sat May 3 23:48:06 2008
