3j4k
From Proteopedia
(Difference between revisions)
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| - | + | ==Cryo-EM structures of the actin:tropomyosin filament reveal the mechanism for the transition from C- to M-state== | |
| - | + | <StructureSection load='3j4k' size='340' side='right' caption='[[3j4k]], [[Resolution|resolution]] 8.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3j4k]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick] 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=3J4K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J4K FirstGlance]. <br> | |
| - | ==Function== | + | </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></td></tr> |
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=3j4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j4k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j4k RCSB], [http://www.ebi.ac.uk/pdbsum/3j4k PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | [[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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tropomyosin (Tm) is a key factor in the molecular mechanisms that regulate the binding of myosin motors to actin filaments (F-Actins) in most eukaryotic cells. This regulation is achieved by the azimuthal repositioning of Tm along the actin (Ac):Tm:troponin (Tn) thin filament to block or expose myosin binding sites on Ac. In striated muscle, including involuntary cardiac muscle, Tm regulates muscle contraction by coupling Ca2+ binding to Tn with myosin binding to the thin filament. In smooth muscle, the switch is the posttranslational modification of the myosin. Depending on the activation state of Tn and the binding state of myosin, Tm can occupy the blocked, closed, or open position on Ac. Using native cryogenic 3DEM (three-dimensional electron microscopy), we have directly resolved and visualized cardiac and gizzard muscle Tm on filamentous Ac in the position that corresponds to the closed state. From the 8-A-resolution structure of the reconstituted Ac:Tm filament formed with gizzard-derived Tm, we discuss two possible mechanisms for the transition from closed to open state and describe the role Tm plays in blocking myosin tight binding in the closed-state position. | ||
| + | |||
| + | Cryo-EM Structures of the Actin:Tropomyosin Filament Reveal the Mechanism for the Transition from C- to M-State.,Sousa DR, Stagg SM, Stroupe ME J Mol Biol. 2013 Sep 8. pii: S0022-2836(13)00540-8. doi:, 10.1016/j.jmb.2013.08.020. PMID:24021812<ref>PMID:24021812</ref> | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Tropomyosin|Tropomyosin]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Chick]] | [[Category: Chick]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| - | [[Category: Sousa, D R | + | [[Category: Sousa, D R]] |
| - | [[Category: Stagg, S M | + | [[Category: Stagg, S M]] |
| - | [[Category: Stroupe, M E | + | [[Category: Stroupe, M E]] |
[[Category: Actin]] | [[Category: Actin]] | ||
[[Category: Coiled-coil c-state]] | [[Category: Coiled-coil c-state]] | ||
[[Category: Structural protein]] | [[Category: Structural protein]] | ||
[[Category: Tropomyosin]] | [[Category: Tropomyosin]] | ||
Revision as of 19:26, 25 December 2014
Cryo-EM structures of the actin:tropomyosin filament reveal the mechanism for the transition from C- to M-state
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