1el6

STRUCTURE OF BACTERIOPHAGE T4 GENE PRODUCT 11, THE INTERFACE BETWEEN THE BASEPLATE AND SHORT TAIL FIBERS

spinqualitylabelsall models 1el6, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1el6 is a 3 chain structure with sequence from Bpt4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VG11_BPT4] Structural component of the baseplate. Connects the short tail fibers to the baseplate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Bacteriophage T4, like all other viruses, is required to be stable while being transmitted from host to host, but also is poised to eject efficiently and rapidly its double-stranded DNA genome to initiate infection. The latter is coordinated by the recognition of receptors on Escherichia coli cells by the long tail fibers and subsequent irreversible attachment by the short tail fibers. These fibers are attached to the baseplate, a multi-subunit assembly at the distal end of the tail. Recognition and attachment induce a conformational transition of the baseplate from a hexagonal to a star-shaped structure.The crystal structure of gene product 11 (gp11), a protein that connects the short tail fibers to the baseplate, has been determined to 2.0 A resolution using multiple wavelength anomalous dispersion with Se. This structure is compared to the trimeric structure of gp9, which connects the baseplate with the long tail fibers. The structure of gp11 is a trimer with each monomer consisting of 218 residues folded into three domains. The N-terminal domains form a central, trimeric, parallel coiled coil surrounded by the middle "finger" domains. The fingers emanate from the carboxy-terminal beta-annulus domain, which, by comparison with the T4 whisker "fibritin" protein, is probably responsible for trimerization. The events leading from recognition of the host to the ejection of viral DNA must be communicated along the assembled trimeric (gp9)(3) attached to the long tail fibers via the trimeric baseplate protein (gp10)(3) to the trimeric (gp11)(3) and the trimeric short tail fibers. Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers.,Leiman PG, Kostyuchenko VA, Shneider MM, Kurochkina LP, Mesyanzhinov VV, Rossmann MG J Mol Biol. 2000 Aug 25;301(4):975-85. PMID:10966799 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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