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| | <SX load='5jlf' size='340' side='right' viewer='molstar' caption='[[5jlf]], [[Resolution|resolution]] 3.60Å' scene=''> | | <SX load='5jlf' size='340' side='right' viewer='molstar' caption='[[5jlf]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jlf]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JLF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JLF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jlf]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JLF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jlf OCA], [http://pdbe.org/5jlf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jlf RCSB], [http://www.ebi.ac.uk/pdbsum/5jlf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jlf ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jlf OCA], [https://pdbe.org/5jlf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jlf RCSB], [https://www.ebi.ac.uk/pdbsum/5jlf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jlf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | + | [https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| | [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Ecken, J von der]]
| + | [[Category: Raunser S]] |
| - | [[Category: Raunser, S]] | + | [[Category: Von der Ecken J]] |
| - | [[Category: Contractile filament]] | + | |
| - | [[Category: Contractile protein]]
| + | |
| - | [[Category: Cryo em]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: F-actin]]
| + | |
| - | [[Category: Filament]]
| + | |
| - | [[Category: Hydrolase complex]]
| + | |
| - | [[Category: Muscle]]
| + | |
| - | [[Category: Protein polymer]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Thin filament]]
| + | |
| - | [[Category: Tropomyosin]]
| + | |
| Structural highlights
Function
ACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Publication Abstract from PubMed
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 A. 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.
Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution.,von der Ecken J, Heissler SM, Pathan-Chhatbar S, Manstein DJ, Raunser S Nature. 2016 Jun 30;534(7609):724-8. PMID:27324845[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ von der Ecken J, Heissler SM, Pathan-Chhatbar S, Manstein DJ, Raunser S. Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution. Nature. 2016 Jun 30;534(7609):724-8. PMID:27324845 doi:http://dx.doi.org/10.1038/nature18295
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