4BLF
Variable internal flexibility characterizes the helical capsid formed by Agrobacterium VirE2 protein on single-stranded DNA.
Summary for 4BLF
| Entry DOI | 10.2210/pdb4blf/pdb |
| EMDB information | 2339 |
| Descriptor | SINGLE-STRAND DNA-BINDING PROTEIN (1 entity in total) |
| Functional Keywords | dna binding protein, tcomplex, agrobacterium, helical reconstruction |
| Biological source | AGROBACTERIUM TUMEFACIENS |
| Cellular location | Secreted : P08062 |
| Total number of polymer chains | 1 |
| Total formula weight | 26667.94 |
| Authors | Bharat, T.A.M.,Zbaida, D.,Eisenstein, M.,Frankenstein, Z.,Mehlman, T.,Weiner, L.,Sorzano, C.O.S.,Barak, Y.,Albeck, S.,Briggs, J.A.G.,Wolf, S.G.,Elbaum, M. (deposition date: 2013-05-02, release date: 2013-06-26, Last modification date: 2024-05-08) |
| Primary citation | Bharat, T.A.M.,Zbaida, D.,Eisenstein, M.,Frankenstein, Z.,Mehlman, T.,Weiner, L.,Sorzano, C.O.S.,Barak, Y.,Albeck, S.,Briggs, J.A.G.,Wolf, S.G.,Elbaum, M. Variable Internal Flexibility Characterizes the Helical Capsid Formed by Agrobacterium Vire2 Protein on Single-Stranded DNA. Structure, 21:1158-, 2013 Cited by PubMed Abstract: 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. PubMed: 23769668DOI: 10.1016/J.STR.2013.04.027 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (20 Å) |
Structure validation
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