5iv5 | pdb_00005iv5

Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex

Loading... Status: waiting for Mol* initialization Structural highlights 5iv5 is a 145 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, ZN Activity: Lysozyme, with EC number 3.2.1.17 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BP11_BPT4] Baseplate protein that is part of the baseplate wedge and that connects the short tail fibers to the baseplate (PubMed:15315755). Involved in the tail assembly. [BP53_BPT4] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly. [BP08_BPT4] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly. [FIB12_BPT4] Structural component of the short tail fiber. Adhesion protein that binds irreversibly to the lipopolysaccharides component (LPS) on the cell surface of Escherichia coli B strains during virus attachment. After at least three long tail fibers have bound, short tail fibers extend and bind irreversibly to the core region of the host cell LPS. [BP25_BPT4] Baseplate protein that is part of the outer wedges of the baseplate (PubMed:15315755). Probably plays a role as a connector between the central and peripheral parts of the baseplate. Involved in the tail assembly.[UniProtKB:P51768] [BP07_BPT4] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly. [BP54_BPT4] Baseplate protein that is part of the baseplate-tail tube junction. Morphogenesis of the baseplate is completed by association of gp48 and gp54, allowing the initiation of the tail-tube polymerization. Involved in the tail assembly. [BP27_BPT4] Baseplate protein that is part of the baseplate hub. Involved in the tail assembly. [TUBE_BPT4] Structural component of the bacteriophage tail which consists of a contractile sheath, a tube and a baseplate. The central cylindrical segment of the tail consists of a rigid tube, composed of multiple copies of gp19, surrounded by the outer contractile sheath assembled from gp18 subunits. During infection, contraction of the sheath drives the central tube through the host outer membrane, creating a channel for DNA ejection from the capsid into the host cell. [BP09_BPT4] Baseplate protein that connects the long tail fibers to the baseplate and probably triggers the tail contraction after virus attachment to a host cell (PubMed:10545330). Involved in the tail assembly (PubMed:21129200). [BP06_BPT4] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly. [BP48_BPT4] Baseplate protein that is part of the baseplate-tail tube junction. Morphogenesis of the baseplate is completed by association of gp48 and gp54, allowing the initiation of the tail-tube polymerization. Involved in the tail assembly. [NEEDL_BPT4] Tail-associated lysozyme of the baseplate hub that is essential for localized hydrolysis of bacterial cell wall necessary for viral DNA injection. The needle-like gp5 protein punctures the outer cell membrane and then digests the peptidoglycan cell wall in the periplasmic space. Involved in the tail assembly. [BP10_BPT4] Baseplate protein that is part of the baseplate wedge and that connects the short tail fibers to the baseplate (PubMed:16554069). During infection, the baseplate undergoes a conformational change from a dome-shaped to a star-shaped structure. At this point, gp10 rotates and acts as a lever that unfolds the short tail fibers, which then interact with host cell surface receptors. Involved in the tail assembly. Publication Abstract from PubMed Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved. Structure of the T4 baseplate and its function in triggering sheath contraction.,Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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