2xyy | pdb_00002xyy

De Novo model of Bacteriophage P22 procapsid coat protein

spinqualitylabelsall models 2xyy, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xyy is a 7 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2xyz Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CAPSD_BPP22] Assembles to form an icosahedral capsid with a T=7 symmetry. Publication Abstract from PubMed Formation of many dsDNA viruses begins with the assembly of a procapsid, containing scaffolding proteins and a multisubunit portal but lacking DNA, which matures into an infectious virion. This process, conserved among dsDNA viruses such as herpes viruses and bacteriophages, is key to forming infectious virions. Bacteriophage P22 has served as a model system for this study in the past several decades. However, how capsid assembly is initiated, where and how scaffolding proteins bind to coat proteins in the procapsid, and the conformational changes upon capsid maturation still remain elusive. Here, we report Calpha backbone models for the P22 procapsid and infectious virion derived from electron cryomicroscopy density maps determined at 3.8- and 4.0-A resolution, respectively, and the first procapsid structure at subnanometer resolution without imposing symmetry. The procapsid structures show the scaffolding protein interacting electrostatically with the N terminus (N arm) of the coat protein through its C-terminal helix-loop-helix motif, as well as unexpected interactions between 10 scaffolding proteins and the 12-fold portal located at a unique vertex. These suggest a critical role for the scaffolding proteins both in initiating the capsid assembly at the portal vertex and propagating its growth on a T = 7 icosahedral lattice. Comparison of the procapsid and the virion backbone models reveals coordinated and complex conformational changes. These structural observations allow us to propose a more detailed molecular mechanism for the scaffolding-mediated capsid assembly initiation including portal incorporation, release of scaffolding proteins upon DNA packaging, and maturation into infectious virions. Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus.,Chen DH, Baker ML, Hryc CF, Dimaio F, Jakana J, Wu W, Dougherty M, Haase-Pettingell C, Schmid MF, Jiang W, Baker D, King JA, Chiu W Proc Natl Acad Sci U S A. 2011 Jan 25;108(4):1355-60. Epub 2011 Jan 10. PMID:21220301 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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