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5MVY

Thin Filament at low calcium concentration

Summary for 5MVY
Entry DOI10.2210/pdb5mvy/pdb
EMDB information3576 3578
DescriptorActin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
Functional Keywordsthin filament, troponin, actin, tropomyosin, structural protein
Biological sourceOryctolagus cuniculus (Rabbit)
Total number of polymer chains23
Total formula weight972965.18
Authors
Paul, D.M.,Squire, J.M.,Morris, E.P. (deposition date: 2017-01-17, release date: 2018-02-14, Last modification date: 2025-04-09)
Primary citationPaul, D.M.,Squire, J.M.,Morris, E.P.
Relaxed and active thin filament structures; a new structural basis for the regulatory mechanism.
J. Struct. Biol., 197:365-371, 2017
Cited by
PubMed Abstract: The structures of muscle thin filaments reconstituted using skeletal actin and cardiac troponin and tropomyosin have been determined with and without bound Ca using electron microscopy and reference-free single particle analysis. The resulting density maps have been fitted with atomic models of actin, tropomyosin and troponin showing that: (i) the polarity of the troponin complex is consistent with our 2009 findings, with large shape changes in troponin between the two states; (ii) without Ca the tropomyosin pseudo-repeats all lie at almost equivalent positions in the 'blocked' position on actin (over subdomains 1 and 2); (iii) in the active state the tropomyosin pseudo-repeats are all displaced towards subdomains 3 and 4 of actin, but the extent of displacement varies within the regulatory unit depending upon the axial location of the pseudo-repeats with respect to troponin. Individual pseudo-repeats with Ca bound to troponin can be assigned either to the 'closed' state, a partly activated conformation, or the 'M-state', a fully activated conformation which has previously been thought to occur only when myosin heads bind. These results lead to a modified view of the steric blocking model of thin filament regulation in which cooperative activation is governed by troponin-mediated local interactions of the pseudo-repeats of tropomyosin with actin.
PubMed: 28161413
DOI: 10.1016/j.jsb.2017.01.004
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (28.4 Å)
Structure validation

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