Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair.

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-incisio

SUBMITTER: Truglio JJ 

PROVIDER: S-EPMC449773 | biostudies-literature | 2004 Jul

REPOSITORIES: biostudies-literature