1AA0
FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)
Summary for 1AA0
| Entry DOI | 10.2210/pdb1aa0/pdb |
| Descriptor | FIBRITIN, CHLORIDE ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | bacteriophage t4, fibritin, structural protein, bacteriophage assembly, attachment protein |
| Biological source | Enterobacteria phage T4 |
| Total number of polymer chains | 1 |
| Total formula weight | 11959.84 |
| Authors | Tao, Y.,Strelkov, S.V.,Mesyanzhinov, V.V.,Rossmann, M.G. (deposition date: 1997-01-18, release date: 1997-07-23, Last modification date: 2024-02-07) |
| Primary citation | Tao, Y.,Strelkov, S.V.,Mesyanzhinov, V.V.,Rossmann, M.G. Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure, 5:789-798, 1997 Cited by PubMed Abstract: Oligomeric coiled-coil motifs are found in numerous protein structures; among them is fibritin, a structural protein of bacteriophage T4, which belongs to a class of chaperones that catalyze a specific phage-assembly process. Fibritin promotes the assembly of the long tail fibers and their subsequent attachment to the tail baseplate; it is also a sensing device that controls the retraction of the long tail fibers in adverse environments and, thus, prevents infection. The structure of fibritin had been predicted from sequence and biochemical analyses to be mainly a triple-helical coiled coil. The determination of its structure at atomic resolution was expected to give insights into the assembly process and biological function of fibritin, and the properties of modified coiled-coil structures in general. PubMed: 9261070DOI: 10.1016/S0969-2126(97)00233-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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