Ontology highlight
ABSTRACT:
SUBMITTER: Lu J
PROVIDER: S-EPMC2700979 | biostudies-literature | 2009 Jun
REPOSITORIES: biostudies-literature
Lu Jun J den Dulk-Ras Amke A Hooykaas Paul J J PJ Glover J N Mark JN
Proceedings of the National Academy of Sciences of the United States of America 20090529 24
Agrobacterium tumefaciens VirC2 stimulates processing of single-stranded T-DNA that is translocated into plants to induce tumor formation, but how VirC2 functions is unclear. Here, we report the 1.7-A X-ray crystal structure of its trypsin-resistant C-terminal domain, VirC2(82-202), which reveals a form of the ribbon-helix-helix (RHH) DNA-binding fold contained within a single polypeptide chain. DNA-binding assays and mutagenesis indicate that VirC2 uses this RHH fold to bind double-stranded DNA ...[more]