2HI5
Model for bacteriophage fd from cryo-EM
Summary for 2HI5
| Entry DOI | 10.2210/pdb2hi5/pdb |
| EMDB information | 1240 |
| Descriptor | Coat protein B (1 entity in total) |
| Functional Keywords | helix, helical virus, structural protein, dna binding protein, virus |
| Biological source | Enterobacteria phage fd |
| Total number of polymer chains | 1 |
| Total formula weight | 5244.00 |
| Authors | Wang, Y.A.,Yu, X.,Overman, S.,Tsuboi, M.,Thomas, G.J.,Egelman, E.H. (deposition date: 2006-06-29, release date: 2007-08-07, Last modification date: 2024-02-14) |
| Primary citation | Wang, Y.A.,Yu, X.,Overman, S.,Tsuboi, M.,Thomas, G.J.,Egelman, E.H. The Structure of a Filamentous Bacteriophage J.Mol.Biol., 361:209-215, 2006 Cited by PubMed Abstract: Many thin helical polymers, including bacterial pili and filamentous bacteriophage, have been seen as refractory to high-resolution studies by electron microscopy. Studies of the quaternary structure of such filaments have depended upon techniques such as modeling or X-ray fiber diffraction, given that direct visualization of the subunit organization has not been possible. We report the first image reconstruction of a filamentous virus, bacteriophage fd, by cryoelectron microscopy. Although these thin ( approximately 70 A in diameter) rather featureless filaments scatter weakly, we have been able to achieve a nominal resolution of approximately 8 A using an iterative helical reconstruction procedure. We show that two different conformations of the virus exist, and that in both states the subunits are packed differently than in conflicting models previously proposed on the basis of X-ray fiber diffraction or solid-state NMR studies. A significant fraction of the population of wild-type fd is either disordered or in multiple conformational states, while in the presence of the Y21M mutation, this heterogeneity is greatly reduced, consistent with previous observations. These results show that new computational approaches to helical reconstruction can greatly extend the ability to visualize heterogeneous protein polymers at a reasonably high resolution. PubMed: 16843489DOI: 10.1016/j.jmb.2006.06.027 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8 Å) |
Structure validation
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