2vvd | pdb_00002vvd

Crystal structure of the receptor binding domain of the spike protein P1 from bacteriophage PM2

spinqualitylabelsall models 2vvd, resolution 2.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vvd is a 1 chain structure with sequence from Alteromonas phage pm2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA NonStd Res: MSE Related: 2vve, 2w0c Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SPIKE_BPPM2] Receptor binding protein located at the fivefold vertices. Publication Abstract from PubMed Recent, primarily structural observations indicate that related viruses, harboring no sequence similarity, infect hosts of different domains of life. One such clade of viruses, defined by common capsid architecture and coat protein fold, is the so-called PRD1-adenovirus lineage. Here we report the structure of the marine lipid-containing bacteriophage PM2 determined by crystallographic analyses of the entire approximately 45 MDa virion and of the outer coat proteins P1 and P2, revealing PM2 to be a primeval member of the PRD1-adenovirus lineage with an icosahedral shell and canonical double beta barrel major coat protein. The view of the lipid bilayer, richly decorated with membrane proteins, constitutes a rare visualization of an in vivo membrane. The viral membrane proteins P3 and P6 are organized into a lattice, suggesting a possible assembly pathway to produce the mature virus. Insights into virus evolution and membrane biogenesis from the structure of the marine lipid-containing bacteriophage PM2.,Abrescia NG, Grimes JM, Kivela HM, Assenberg R, Sutton GC, Butcher SJ, Bamford JK, Bamford DH, Stuart DI Mol Cell. 2008 Sep 5;31(5):749-61. PMID:18775333 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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