Structural Insights into the Cryptic DNA-dependent ATPase Activity of UvrB

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...

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Veröffentlicht in:	Journal of molecular biology 2006-03, Vol.357 (1), p.62-72
Hauptverfasser:	Eryilmaz, Jitka, Ceschini, Simona, Ryan, James, Geddes, Stella, Waters, Timothy R., Barrett, Tracey E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Diphosphate - chemistry Adenosine Diphosphate - metabolism Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism ADP Bacillus - enzymology Bacillus - genetics Bacillus subtilis - chemistry Bacillus subtilis - enzymology Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism complex Crystallography, X-Ray DNA DNA - chemistry DNA - metabolism DNA Helicases - chemistry DNA Helicases - genetics DNA Helicases - metabolism DNA Repair helicase Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Nucleic Acid Conformation Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Thermus thermophilus - enzymology Thermus thermophilus - genetics UvrB
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