4GBF
Crystal structure of the C-terminal domain of gp131 from bacteriophage phiKZ
Summary for 4GBF
| Entry DOI | 10.2210/pdb4gbf/pdb |
| Descriptor | PHIKZ131, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | 7-bladed beta-propeller, possibly participates in binding of the phage to the host cell, at the periphery of the baseplate or in the fiber of bacteriophage phikz, viral protein |
| Biological source | Pseudomonas phage phiKZ |
| Total number of polymer chains | 2 |
| Total formula weight | 88192.68 |
| Authors | Sycheva, L.V.,Shneider, M.M.,Leiman, P.G. (deposition date: 2012-07-27, release date: 2012-10-17, Last modification date: 2024-02-28) |
| Primary citation | Sycheva, L.V.,Shneider, M.M.,Sykilinda, N.N.,Ivanova, M.A.,Miroshnikov, K.A.,Leiman, P.G. Crystal structure and location of gp131 in the bacteriophage phiKZ virion. Virology, 434:257-264, 2012 Cited by PubMed Abstract: Pseudomonas phage ϕKZ and its two close relatives ϕPA3 and 201ϕ2-1 are very large bacteriophages that form a separate branch in phage classification because their genomes are very different from the rest of GenBank sequence data. The contractile tail of ϕKZ is built from at least 32 different proteins, but a definitive structural function is assigned to only one of them-the tail sheath protein. Here, we report the crystal structure of the C-terminal domain of another phiKZ tail protein, gene product 131 (gp131C). We show that gp131 is located at the periphery of the baseplate and possibly associates with fibers that emanate from the baseplate. Gp131C is a seven-bladed β-propeller that has a shape of a skewed toroid. A small but highly conserved and negatively charged patch on the surface of gp131C might be important for substrate binding or for interaction with a different tail protein. PubMed: 23031178DOI: 10.1016/j.virol.2012.09.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.949 Å) |
Structure validation
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