2wzp

STRUCTURES OF LACTOCOCCAL PHAGE P2 BASEPLATE SHED LIGHT ON A NOVEL MECHANISM OF HOST ATTACHMENT AND ACTIVATION IN SIPHOVIRIDAE

spinqualitylabelsall models 2wzp, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wzp is a 15 chain structure with sequence from Lactococcus phage p2 and Lama glama. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1zru, 2bsd, 2bse Resources: FirstGlance, OCA, RCSB, PDBsum 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 Siphoviridae is the most abundant viral family on earth which infects bacteria as well as archaea. All known siphophages infecting gram+ Lactococcus lactis possess a baseplate at the tip of their tail involved in host recognition and attachment. Here, we report analysis of the p2 phage baseplate structure by X-ray crystallography and electron microscopy and propose a mechanism for the baseplate activation during attachment to the host cell. This approximately 1 MDa, Escherichia coli-expressed baseplate is composed of three protein species, including six trimers of the receptor-binding protein (RBP). RBPs host-recognition domains point upwards, towards the capsid, in agreement with the electron-microscopy map of the free virion. In the presence of Ca(2+), a cation mandatory for infection, the RBPs rotated 200 degrees downwards, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA passage. These conformational changes reveal a novel siphophage activation and host-recognition mechanism leading ultimately to DNA ejection. Structure of lactococcal phage p2 baseplate and its mechanism of activation.,Sciara G, Bebeacua C, Bron P, Tremblay D, Ortiz-Lombardia M, Lichiere J, van Heel M, Campanacci V, Moineau S, Cambillau C Proc Natl Acad Sci U S A. 2010 Mar 29. PMID:20351260 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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