Eryilmaz, Jitka and Ceschini, Simona and Ryan, James and Geddes, Stella M. and Waters, Timothy R. and Barrett, Tracey E. (2006) Structural insights into the cryptic DNA-dependent ATPase activity of UvrB. Journal of Molecular Biology 357 (1), pp. 62-72. ISSN 0022-2836.Full text not available from this repository.
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 β-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 β-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.
|Keyword(s) / Subject(s):||UvrB, helicase, DNA, ADP, complex|
|School or Research Centre:||Birkbeck Schools and Research Centres > School of Science > Biological Sciences|
|Date Deposited:||18 Aug 2011 10:59|
|Last Modified:||17 Apr 2013 12:21|
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