5muu | pdb_00005muu

dsRNA bacteriophage phi6 nucleocapsid

spinqualitylabelsall models 5muu, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5muu is a 13 chain structure with sequence from Pseudomonas phage phi6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Nucleoside-triphosphatase, with EC number 3.6.1.15 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [P1_BPPH6] P1 is the major inner capsid (core) protein of the polyhedral procapsid, which is responsible for genomic replication and transcription. Forms a dodecahedral shell from 60 asymmetric dimers. Binds to RNA and may be involved in genomic packaging. [CAPSD_BPPH6] Assembles to form an icosahedral capsid with a T=13 symmetry. Drives the penetration of the inner capsid (core) into the cytoplasm. [P4_BPPH6] P4 is one of the structural proteins of the polyhedral procapsid, which is responsible for genomic replication and transcription. Displays single-stranded RNA-stimulated NTPase activity. Publication Abstract from PubMed Correct outer protein shell assembly is a prerequisite for virion infectivity in many multi-shelled dsRNA viruses. In the prototypic dsRNA bacteriophage phi6, the assembly reaction is promoted by calcium ions but its biomechanics remain poorly understood. Here, we describe the near-atomic resolution structure of the phi6 double-shelled particle. The outer T=13 shell protein P8 consists of two alpha-helical domains joined by a linker, which allows the trimer to adopt either a closed or an open conformation. The trimers in an open conformation swap domains with each other. Our observations allow us to propose a mechanistic model for calcium concentration regulated outer shell assembly. Furthermore, the structure provides a prime exemplar of bona fide domain-swapping. This leads us to extend the theory of domain-swapping from the level of monomeric subunits and multimers to closed spherical shells, and to hypothesize a mechanism by which closed protein shells may arise in evolution. Double-stranded RNA virus outer shell assembly by bona fide domain-swapping.,Sun Z, El Omari K, Sun X, Ilca SL, Kotecha A, Stuart DI, Poranen MM, Huiskonen JT Nat Commun. 2017 Mar 13;8:14814. doi: 10.1038/ncomms14814. PMID:28287099 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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