5WJB
Crystal Structure of Amino Acids 1733-1797 of Human Beta Cardiac Myosin Fused to Gp7
5WJB の概要
エントリーDOI | 10.2210/pdb5wjb/pdb |
分子名称 | Capsid assembly scaffolding protein,Myosin-7 (2 entities in total) |
機能のキーワード | myosin, gp7, coiled-coil, actin-dna binding protein complex, actin/dna binding protein |
由来する生物種 | Bacillus phage phi29 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 63630.47 |
構造登録者 | Andreas, M.P.,Ajay, G.,Gellings, J.,Rayment, I. (登録日: 2017-07-21, 公開日: 2017-08-09, 最終更新日: 2023-10-04) |
主引用文献 | Andreas, M.P.,Ajay, G.,Gellings, J.A.,Rayment, I. Design considerations in coiled-coil fusion constructs for the structural determination of a problematic region of the human cardiac myosin rod. J. Struct. Biol., 200:219-228, 2017 Cited by PubMed Abstract: X-ray structural determination of segments of the myosin rod has proved difficult because of the strong salt-dependent aggregation properties and repeating pattern of charges on the surface of the coiled-coil that lead to the formation of paracrystals. This problem has been resolved in part through the use of globular assembly domains that improve protein folding and prevent aggregation. The primary consideration now in designing coiled-coil fusion constructs for myosin is deciding where to truncate the coiled-coil and which amino acid residues to include from the folding domain. This is especially important for myosin that contains numerous regions of low predicted coiled-coil propensity. Here we describe the strategy adopted to determine the structure of the region that extends from Arg1677 - Leu1797 that included two areas that do not show a strong sequence signature of a conventional left-handed coiled coil or canonical heptad repeat. This demonstrates again that, with careful choice of fusion constructs, overlapping structures exhibit very similar conformations for the myosin rod fragments in the canonical regions. However, conformational variability is seen around Leu1706 which is a hot spot for cardiomyopathy mutations suggesting that this might be important for function. PubMed: 28743637DOI: 10.1016/j.jsb.2017.07.006 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.905 Å) |
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