3vtn | pdb_00003vtn

The crystal structure of the C-terminal domain of Mu phage central spike - Pt derivative for MAD

spinqualitylabelsall models 3vtn, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vtn is a 1 chain structure with sequence from Bpmu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, PT Related: 3vto Gene: 45 (BPMU) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BP45_BPMU] Component of the baseplate that forms a central needlelike spike used to puncture the host cell membrane for tube insertion during virus entry. Probably involved in baseplate and tail assembly. Serves as the distal plug of tail tube channel and might regulate the process of the phage DNA and protein ejection into the host cell. Publication Abstract from PubMed Bacteriophage Mu, which has a contractile tail, is one of the most famous genus of Myoviridae. It has a wide host range and is thought to contribute to horizontal gene transfer. The Myoviridae infection process is initiated by adhesion to the host surface. The phage then penetrates the host cell membrane using its tail to inject its genetic material into the host. In this penetration process, Myoviridae phages are proposed to puncture the membrane of the host cell using a central spike located beneath its baseplate. The central spike of the Mu phage is thought to be composed of gene 45 product (gp45), which has a significant sequence homology with the central spike of P2 phage (gpV). We determined the crystal structure of shortened Mu gp45Delta1-91 (Arg92-Gln197) at 1.5A resolution and showed that Mu gp45 is a needlelike structure that punctures the membrane. The apex of Mu gp45 and that of P2 gpV contained iron, chloride, and calcium ions. Although the C-terminal domain of Mu gp45 was sufficient for binding to the E. coli membrane, a mutant D188A, in which the Asp amino acid residue that coordinates the calcium ion was replaced by Ala, did not exhibit a propensity to bind to the membrane. Therefore, we concluded that calcium ion played an important role in interaction with the host cell membrane. Crystal structure of the C-terminal domain of Mu phage central spike and functions of bound calcium ion.,Harada K, Yamashita E, Nakagawa A, Miyafusa T, Tsumoto K, Ueno T, Toyama Y, Takeda S Biochim Biophys Acta. 2013 Jan;1834(1):284-91. doi: 10.1016/j.bbapap.2012.08.015., Epub 2012 Aug 24. PMID:22922659 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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