2RH3

Crystal structure of plasmid pTiC58 VirC2

Summary for 2RH3

• Entry DOI: 10.2210/pdb2rh3/pdb
• Descriptor: Protein virC2 (2 entities in total)
• Functional Keywords: ribbon-helix-helix, protein, crown gall tumor, dna binding protein
• Biological source: Agrobacterium tumefaciens
• Total number of polymer chains: 1
• Total formula weight: 13413.48

Authors

Lu, J.,Glover, J.N.M. (deposition date: 2007-10-05, release date: 2008-10-14, Last modification date: 2024-02-21)

Primary citation

Lu, J.,den Dulk-Ras, A.,Hooykaas, P.J.,Glover, J.N.
Agrobacterium tumefaciens VirC2 enhances T-DNA transfer and virulence through its C-terminal ribbon-helix-helix DNA-binding fold
Proc.Natl.Acad.Sci.USA, 106:9643-9648, 2009

PubMed Abstract: 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 but not single-stranded DNA. Mutations that severely affect VirC2 DNA binding are highly deleterious for both T-DNA transfer into yeast and the virulence of A. tumefaciens in different plants including Nicotiana glauca and Kalanchoe daigremontiana. These data suggest that VirC2 enhances T-DNA transfer and virulence through DNA binding with its RHH fold. The RHH fold of VirC2 is the first crystal structure representing a group of predicted RHH proteins that facilitate endonucleolytic processing of DNA for horizontal gene transfer.

PubMed: 19482939
DOI: 10.1073/pnas.0812199106

Experimental method

X-RAY DIFFRACTION (1.7 Å)