Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair

• Published in: The EMBO journal Vol. 18; no. 24; pp. 6899 - 6907
• Main Authors: Theis, Karsten, Chen, Paul J., Skorvaga, Milan, Van Houten, Bennett, Kisker, Caroline
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 15.12.1999; Blackwell Publishing Ltd
• Subjects: Adenosine Triphosphate - metabolism; Amino Acid Sequence; Bacillus - enzymology; Bacillus - genetics; Binding Sites; crystallography; Crystallography, X-Ray - methods; DNA Damage; DNA helicase; DNA Helicases - chemistry; DNA Helicases - metabolism; DNA Repair; helicase; Models, Molecular; Molecular Sequence Data; nucleotide excision repair; Protein Structure, Secondary; Sequence Alignment; Sequence Homology, Amino Acid; UvrB; UvrB protein
• ISSN: 0261-4189; 1460-2075; 1460-2075
• DOI: 10.1093/emboj/18.24.6899

Nucleotide excision repair (NER) is a highly conserved DNA repair mechanism. NER systems recognize the damaged DNA strand, cleave it on both sides of the lesion, remove and newly synthesize the fragment. UvrB is a central component of the bacterial NER system participating in damage recognition, strand excision and repair synthesis. We have solved the crystal structure of UvrB in the apo and the ATP‐bound forms. UvrB contains two domains related in structure to helicases, and two additional domains unique to repair proteins. The structure contains all elements of an intact helicase, and is evidence that UvrB utilizes ATP hydrolysis to move along the DNA to probe for damage. The location of conserved residues and structural comparisons allow us to predict the path of the DNA and suggest that the tight pre‐incision complex of UvrB and the damaged DNA is formed by insertion of a flexible β‐hairpin between the two DNA strands.