1T5L

Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2

Summary for 1T5L

• Entry DOI: 10.2210/pdb1t5l/pdb
• Related: 1C40 1D2M 1D9X 1D9Z 1E52 1QOJ
• Descriptor: UvrABC system protein B, ZINC ION (3 entities in total)
• Functional Keywords: dna damage, dna repair, nucleotide excision repair, uvrb, uvra, uvrc, ner, mfd, trcf, dna excision repair
• Biological source: Bacillus caldotenax
• Cellular location: Cytoplasm (By similarity): P56981
• Total number of polymer chains: 2
• Total formula weight: 151251.45

Authors

Truglio, J.J.,Croteau, D.L.,Skorvaga, M.,DellaVecchia, M.J.,Theis, K.,Mandavilli, B.S.,Van Houten, B.,Kisker, C. (deposition date: 2004-05-04, release date: 2004-06-22, Last modification date: 2024-02-14)

Primary citation

Truglio, J.J.,Croteau, D.L.,Skorvaga, M.,DellaVecchia, M.J.,Theis, K.,Mandavilli, B.S.,Van Houten, B.,Kisker, C.
Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair
Embo J., 23:2498-2509, 2004

PubMed Abstract: Nucleotide excision repair (NER) is a highly conserved DNA repair mechanism present in all kingdoms of life. UvrB is a central component of the bacterial NER system, participating in damage recognition, strand excision and repair synthesis. None of the three presently available crystal structures of UvrB has defined the structure of domain 2, which is critical for the interaction with UvrA. We have solved the crystal structure of the UvrB Y96A variant, which reveals a new fold for domain 2 and identifies highly conserved residues located on its surface. These residues are restricted to the face of UvrB important for DNA binding and may be critical for the interaction of UvrB with UvrA. We have mutated these residues to study their role in the incision reaction, formation of the pre-incision complex, destabilization of short duplex regions in DNA, binding to UvrA and ATP hydrolysis. Based on the structural and biochemical data, we conclude that domain 2 is required for a productive UvrA-UvrB interaction, which is a pre-requisite for all subsequent steps in nucleotide excision repair.

PubMed: 15192705
DOI: 10.1038/sj.emboj.7600263

Experimental method

X-RAY DIFFRACTION (2.6 Å)