View source for 2w49


==ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE==
<SX load='2w49' size='340' side='right' viewer='molstar' caption='[[2w49]], [[Resolution|resolution]] 35.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2w49]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] 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=2W49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W49 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2w49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w49 OCA], [https://pdbe.org/2w49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w49 RCSB], [https://www.ebi.ac.uk/pdbsum/2w49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w49 ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/TNNC2_CHICK TNNC2_CHICK] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w4/2w49_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2w49 ConSurf].
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== Publication Abstract from PubMed ==
BACKGROUND: Isometric muscle contraction, where force is generated without muscle shortening, is a molecular traffic jam in which the number of actin-attached motors is maximized and all states of motor action are trapped with consequently high heterogeneity. This heterogeneity is a major limitation to deciphering myosin conformational changes in situ. METHODOLOGY: We used multivariate data analysis to group repeat segments in electron tomograms of isometrically contracting insect flight muscle, mechanically monitored, rapidly frozen, freeze substituted, and thin sectioned. Improved resolution reveals the helical arrangement of F-actin subunits in the thin filament enabling an atomic model to be built into the thin filament density independent of the myosin. Actin-myosin attachments can now be assigned as weak or strong by their motor domain orientation relative to actin. Myosin attachments were quantified everywhere along the thin filament including troponin. Strong binding myosin attachments are found on only four F-actin subunits, the "target zone", situated exactly midway between successive troponin complexes. They show an axial lever arm range of 77 degrees /12.9 nm. The lever arm azimuthal range of strong binding attachments has a highly skewed, 127 degrees range compared with X-ray crystallographic structures. Two types of weak actin attachments are described. One type, found exclusively in the target zone, appears to represent pre-working-stroke intermediates. The other, which contacts tropomyosin rather than actin, is positioned M-ward of the target zone, i.e. the position toward which thin filaments slide during shortening. CONCLUSION: We present a model for the weak to strong transition in the myosin ATPase cycle that incorporates azimuthal movements of the motor domain on actin. Stress/strain in the S2 domain may explain azimuthal lever arm changes in the strong binding attachments. The results support previous conclusions that the weak attachments preceding force generation are very different from strong binding attachments.

Electron tomography of cryofixed, isometrically contracting insect flight muscle reveals novel actin-myosin interactions.,Wu S, Liu J, Reedy MC, Tregear RT, Winkler H, Franzini-Armstrong C, Sasaki H, Lucaveche C, Goldman YE, Reedy MK, Taylor KA PLoS One. 2010 Sep 9;5(9). pii: e12643. PMID:20844746<ref>PMID:20844746</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Actin 3D structures|Actin 3D structures]]
*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
*[[Troponin 3D structures|Troponin 3D structures]]
== References ==
<references/>
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[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Franzini-Armstrong C]]
[[Category: Goldman YE]]
[[Category: Liu J]]
[[Category: Lucaveche C]]
[[Category: Reedy MC]]
[[Category: Reedy MK]]
[[Category: Sasaki H]]
[[Category: Taylor KA]]
[[Category: Tregear RT]]
[[Category: Winkler H]]
[[Category: Wu S]]