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TitleVariable internal flexibility characterizes the helical capsid formed by agrobacterium VirE2 protein on single-stranded DNA.
Journal, issue, pagesStructure, Vol. 21, Issue 7, Page 1158-1167, Year 2013
Publish dateJul 2, 2013
AuthorsTanmay A M Bharat / David Zbaida / Miriam Eisenstein / Ziv Frankenstein / Tevie Mehlman / Lev Weiner / Carlos Oscar S Sorzano / Yoav Barak / Shira Albeck / John A G Briggs / Sharon G Wolf / Michael Elbaum /
PubMed AbstractAgrobacterium is known for gene transfer to plants. In addition to a linear ssDNA oligonucleotide, Agrobacterium tumefaciens secretes an abundant ssDNA-binding effector, VirE2. In many ways VirE2 ...Agrobacterium is known for gene transfer to plants. In addition to a linear ssDNA oligonucleotide, Agrobacterium tumefaciens secretes an abundant ssDNA-binding effector, VirE2. In many ways VirE2 adapts the conjugation mechanism to transform the eukaryotic host. The crystal structure of VirE2 shows two compact domains joined by a flexible linker. Bound to ssDNA, VirE2 forms an ordered solenoidal shell, or capsid known as the T-complex. Here, we present a three-dimensional reconstruction of the VirE2-ssDNA complex using cryo-electron microscopy and iterative helical real-space reconstruction. High-resolution refinement was not possible due to inherent heterogeneity in the protein structure. By a combination of computational modeling, chemical modifications, mass spectroscopy, and electron paramagnetic resonance, we found that the N-terminal domain is tightly constrained by both tangential and longitudinal links, while the C terminus is weakly constrained. The quaternary structure is thus rigidly assembled while remaining locally flexible. This flexibility may be important in accommodating substrates without sequence specificity.
External linksStructure / PubMed:23769668
MethodsEM (helical sym.)
Resolution20.0 Å
Structure data

2339

4blf

EMDB-2339, PDB-4blf:
Variable internal flexibility characterizes the helical capsid formed by Agrobacterium VirE2 protein on single-stranded DNA.
Method: EM (helical sym.) / Resolution: 20.0 Å

Source
  • Agrobacterium fabrum str. C58 (bacteria)
  • agrobacterium tumefaciens (bacteria)
KeywordsDNA BINDING PROTEIN / TCOMPLEX / AGROBACTERIUM / HELICAL RECONSTRUCTION

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