Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution.
Journal, issue, pages	Nature, Vol. 534, Issue 7609, Page 724-728, Year 2016
Publish date	Jun 30, 2016
PubMed Abstract	The interaction of myosin with actin filaments is the central feature of muscle contraction and cargo movement along actin filaments of the cytoskeleton. The energy for these movements is generated ...The interaction of myosin with actin filaments is the central feature of muscle contraction and cargo movement along actin filaments of the cytoskeleton. The energy for these movements is generated during a complex mechanochemical reaction cycle. Crystal structures of myosin in different states have provided important structural insights into the myosin motor cycle when myosin is detached from F-actin. The difficulty of obtaining diffracting crystals, however, has prevented structure determination by crystallography of actomyosin complexes. Thus, although structural models exist of F-actin in complex with various myosins, a high-resolution structure of the F-actin–myosin complex is missing. Here, using electron cryomicroscopy, we present the structure of a human rigor actomyosin complex at an average resolution of 3.9 Å. The structure reveals details of the actomyosin interface, which is mainly stabilized by hydrophobic interactions. The negatively charged amino (N) terminus of actin interacts with a conserved basic motif in loop 2 of myosin, promoting cleft closure in myosin. Surprisingly, the overall structure of myosin is similar to rigor-like myosin structures in the absence of F-actin, indicating that F-actin binding induces only minimal conformational changes in myosin. A comparison with pre-powerstroke and intermediate (Pi-release) states of myosin allows us to discuss the general mechanism of myosin binding to F-actin. Our results serve as a strong foundation for the molecular understanding of cytoskeletal diseases, such as autosomal dominant hearing loss and diseases affecting skeletal and cardiac muscles, in particular nemaline myopathy and hypertrophic cardiomyopathy.
External links	Nature / PubMed:27324845
Methods	EM (single particle)
Resolution	3.6 - 3.9 Å
Structure data	8162 5jlf EMDB-8162: Structure of the F-actin-tropomyosin complex (reprocessed, tropomyosin filtered to 7 Angstrom) PDB-5jlf: Structure of the F-actin-tropomyosin complex (Reprocessed) Method: EM (single particle) / Resolution: 3.6 Å 8163 5jlf EMDB-8163: Structure of the F-actin-tropomyosin complex (reprocessed) PDB-5jlf: Structure of the F-actin-tropomyosin complex (Reprocessed) Method: EM (single particle) / Resolution: 3.6 Å 8164 5jlh EMDB-8164: Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution (tropomyosin filtered to 7 Angstrom) PDB-5jlh: Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution Method: EM (single particle) / Resolution: 3.9 Å 8165 5jlh EMDB-8165, PDB-5jlh: Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution Method: EM (single particle) / Resolution: 3.9 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-MG*: Unknown entry
Source	oryctolagus cuniculus (rabbit) mus musculus (house mouse) Rabbit (rabbit) homo sapiens (human) dictyostelium discoideum (eukaryote)
Keywords	CONTRACTILE PROTEIN / CONTRACTILE FILAMENT / MUSCLE / THIN FILAMENT / CYTOSKELETON / STRUCTURAL PROTEIN / HYDROLASE COMPLEX / F-actin / tropomyosin / filament / protein polymers / cryo EM / myosin