Crystal structure of tropomyosin at 7 Angstroms resolution. Export

@article{citeulike:796404, 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.}, address = {Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005, USA.}, author = {Whitby, F. G. and Phillips, G. N.}, citeulike-article-id = {796404}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/10651038}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=10651038}, day = {1}, issn = {0887-3585}, journal = {Proteins}, keywords = {lox-1, neck\_domain}, month = {January}, number = {1}, pages = {49--59}, posted-at = {2009-01-12 17:31:36}, priority = {2}, title = {Crystal structure of tropomyosin at 7 Angstroms resolution.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/10651038}, volume = {38}, year = {2000} }

TY - JOUR ID - citeulike:796404 L3 - citeulike-article-id:796404 N2 - 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. IS - 1 JF - Proteins SN - 0887-3585 AD - Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005, USA. EP - 59 TI - Crystal structure of tropomyosin at 7 Angstroms resolution. VL - 38 SP - 49 KW - lox-1 KW - neck_domain AU - Whitby, FG AU - Phillips, GN PY - 2000/01/01/ UR - http://view.ncbi.nlm.nih.gov/pubmed/10651038 ER -