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2w4u

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{{Seed}}
 
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[[Image:2w4u.jpg|left|200px]]
 
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==Isometrically contracting insect asynchronous flight muscle quick frozen after a length step==
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The line below this paragraph, containing "STRUCTURE_2w4u", creates the "Structure Box" on the page.
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<SX load='2w4u' size='340' side='right' viewer='molstar' caption='[[2w4u]], [[Resolution|resolution]] 35.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2w4u]] 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=2W4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W4U FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w4u OCA], [https://pdbe.org/2w4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w4u RCSB], [https://www.ebi.ac.uk/pdbsum/2w4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w4u ProSAT]</span></td></tr>
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{{STRUCTURE_2w4u| PDB=2w4u | SCENE= }}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w4/2w4u_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2w4u ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The application of rapidly applied length steps to actively contracting muscle is a classic method for synchronizing the response of myosin cross-bridges so that the average response of the ensemble can be measured. Alternatively, electron tomography (ET) is a technique that can report the structure of the individual members of the ensemble. We probed the structure of active myosin motors (cross-bridges) by applying 0.5% changes in length (either a stretch or a release) within 2 ms to isometrically contracting insect flight muscle (IFM) fibers followed after 5-6 ms by rapid freezing against a liquid helium cooled copper mirror. ET of freeze-substituted fibers, embedded and thin-sectioned, provides 3-D cross-bridge images, sorted by multivariate data analysis into approximately 40 classes, distinct in average structure, population size and lattice distribution. Individual actin subunits are resolved facilitating quasi-atomic modeling of each class average to determine its binding strength (weak or strong) to actin. approximately 98% of strong-binding acto-myosin attachments present after a length perturbation are confined to "target zones" of only two actin subunits located exactly midway between successive troponin complexes along each long-pitch helical repeat of actin. Significant changes in the types, distribution and structure of actin-myosin attachments occurred in a manner consistent with the mechanical transients. Most dramatic is near disappearance, after either length perturbation, of a class of weak-binding cross-bridges, attached within the target zone, that are highly likely to be precursors of strong-binding cross-bridges. These weak-binding cross-bridges were originally observed in isometrically contracting IFM. Their disappearance following a quick stretch or release can be explained by a recent kinetic model for muscle contraction, as behaviour consistent with their identification as precursors of strong-binding cross-bridges. The results provide a detailed model for contraction in IFM that may be applicable to contraction in other types of muscle.
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===ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE QUICK FROZEN AFTER A LENGTH STEP===
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Structural Changes in Isometrically Contracting Insect Flight Muscle Trapped following a Mechanical Perturbation.,Wu S, Liu J, Reedy MC, Perz-Edwards RJ, Tregear RT, Winkler H, Franzini-Armstrong C, Sasaki H, Lucaveche C, Goldman YE, Reedy MK, Taylor KA PLoS One. 2012;7(6):e39422. Epub 2012 Jun 25. PMID:22761792<ref>PMID:22761792</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2w4u" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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2W4U is a 36 chains structure with sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] 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=2W4U OCA].
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*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
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*[[Troponin 3D structures|Troponin 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:19698791</ref><references group="xtra"/>
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<references/>
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__TOC__
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</SX>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Franzini-Armstrong, C.]]
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[[Category: Franzini-Armstrong C]]
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[[Category: Goldman, Y E.]]
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[[Category: Goldman YE]]
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[[Category: Liu, J.]]
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[[Category: Liu J]]
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[[Category: Lucaveche, C.]]
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[[Category: Lucaveche C]]
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[[Category: Reedy, M C.]]
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[[Category: Reedy MC]]
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[[Category: Reedy, M K.]]
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[[Category: Reedy MK]]
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[[Category: Sasaki, H.]]
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[[Category: Sasaki H]]
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[[Category: Taylor, K A.]]
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[[Category: Taylor KA]]
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[[Category: Tregear, R T.]]
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[[Category: Tregear RT]]
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[[Category: Winkler, H.]]
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[[Category: Winkler H]]
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[[Category: Wu, S.]]
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[[Category: Wu S]]
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[[Category: Actin-binding]]
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[[Category: Atp-binding]]
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[[Category: Calmodulin-binding]]
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[[Category: Contractile protein]]
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[[Category: Freeze substitution]]
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[[Category: Isometric contraction]]
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[[Category: Methylation]]
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[[Category: Microtomy]]
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[[Category: Motor protein]]
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[[Category: Muscle protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 25 08:48:05 2010''
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Current revision

Isometrically contracting insect asynchronous flight muscle quick frozen after a length step

2w4u, resolution 35.00Å

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