5cj1

Crystal structure of the coiled coil of MYH7 residues 1526 to 1571 fused to Gp7

spinqualitylabelsall models 5cj1, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cj1 is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5chx, 5cj0, 5cj4 Gene: MYH7, MYHCB (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SCAF_BPPH2] Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid. Publication Abstract from PubMed Sarcomeric myosins have the remarkable ability to form regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. This has been established for over fifty years and yet a molecular model for the thick filament has not been attained. In part this is due to the lack of a detailed molecular model for the coiled-coil that constitutes the myosin rod. The ability to self-assemble resides in the C-terminal of the section of myosin known as light meromyosin (LMM) which exhibits strong salt dependent aggregation that has inhibited structural studies. Here we evaluate the feasibility of generating a complete model for the myosin rod by combining overlapping structures of five sections of coiled-coil covering 164 amino acid residues which constitute 20% of LMM. Each section contains approximately 7-9 heptads of myosin. The problem of aggregation was overcome by incorporating the globular folding domains, Gp7 and Xrcc4 which enhance crystallization. The effect of these domains on the stability and conformation of the myosin rod was examined through biophysical studies and overlapping structures. In addition, a computational approach was developed to combine the sections into a contiguous model. The structures were aligned, trimmed to form a contiguous model, and simulated for >700 ns to remove the discontinuities and achieve an equilibrated conformation that represents the native state. This experimental and computational strategy lays the foundation for building a model for the entire myosin rod. This article is protected by copyright. All rights reserved. A composite approach towards a complete model of the myosin rod.,Korkmaz EN, Taylor KC, Andreas MP, Ajay G, Heinze NT, Cui Q, Rayment I Proteins. 2015 Nov 17. doi: 10.1002/prot.24964. PMID:26573747 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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