1C1G

CRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM

1C1G の概要

• エントリーDOI: 10.2210/pdb1c1g/pdb
• 分子名称: TROPOMYOSIN (1 entity in total)
• 機能のキーワード: tropomyosin coiled-coil alpha-helical, contractile protein
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Cytoplasm, cytoskeleton : P42639
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 131138.55

構造登録者

Whitby, F.G.,Phillips Jr., G.N. (登録日: 1999-07-22, 公開日: 2000-02-11, 最終更新日: 2024-02-07)

主引用文献

Whitby, F.G.,Phillips Jr., G.N.
Crystal structure of tropomyosin at 7 Angstroms resolution.
Proteins, 38:49-59, 2000

PubMed Abstract: Tropomyosin is a 400A-long coiled coil that polymerizes to form a continuous filament that associates with actin in muscle and numerous non-muscle cells. Tropomyosin and troponin together form a calcium-sensitive switch that is responsible for thin-filament regulation of striated muscle. Subtle structural features of the molecule, including non-canonical aspects of its coiled-coil motif, undoubtedly influence its association with f-actin and its role in thin filament regulation. Previously, careful inspection of native diffraction intensities was sufficient to construct a model of tropomyosin at 9A resolution in a spermine-induced crystal form that diffracts anisotropically to 4A resolution. Single isomorphous replacement (SIR) phasing has now provided an empirical determination of the structure at 7A resolution. A novel method of heavy-atom analysis was used to overcome difficulties in interpretation of extremely anisotropic diffraction. The packing arrangement of the molecules in the crystal, and important aspects of the tropomyosin geometry such as non-uniformities of the pitch and variable bending and radius of the coiled coil are evident.

PubMed: 10651038
DOI: 10.1002/(SICI)1097-0134(20000101)38:1<49::AID-PROT6>3.3.CO;2-2

実験手法

X-RAY DIFFRACTION (7 Å)