2w4u: Difference between revisions

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-[[Image:2w4u.png|left|200px]]
-{{STRUCTURE_2w4u|  PDB=2w4u  |  SCENE=  }}
+==Isometrically contracting insect asynchronous flight muscle quick frozen after a length step==
+<SX load='2w4u' size='340' side='right' viewer='molstar' caption='[[2w4u]], [[Resolution|resolution]] 35.00&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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='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>
+</table>
+== 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/w4/2w4u_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=2w4u ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===Isometrically contracting insect asynchronous flight muscle quick frozen after a length step===
+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>
-{{ABSTRACT_PUBMED_22761792}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2w4u" style="background-color:#fffaf0;"></div>
-[[2w4u]] is a 36 chain structure of [[Troponin]] with sequence 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].
 ==See Also==
-*[[Tropomyosin|Tropomyosin]]
+*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
-*[[Troponin|Troponin]]
+*[[Troponin 3D structures|Troponin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:022761792</ref><ref group="xtra">PMID:019698791</ref><references group="xtra"/>
+__TOC__
+</SX>
 [[Category: Gallus gallus]]
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Franzini-Armstrong, C.]]
+[[Category: Franzini-Armstrong C]]
-[[Category: Goldman, Y E.]]
+[[Category: Goldman YE]]
-[[Category: Liu, J.]]
+[[Category: Liu J]]
-[[Category: Lucaveche, C.]]
+[[Category: Lucaveche C]]
-[[Category: Reedy, M C.]]
+[[Category: Reedy MC]]
-[[Category: Reedy, M K.]]
+[[Category: Reedy MK]]
-[[Category: Sasaki, H.]]
+[[Category: Sasaki H]]
-[[Category: Taylor, K A.]]
+[[Category: Taylor KA]]
-[[Category: Tregear, R T.]]
+[[Category: Tregear RT]]
-[[Category: Winkler, H.]]
+[[Category: Winkler H]]
-[[Category: Wu, S.]]
+[[Category: Wu S]]
-[[Category: Actin-binding]]
-[[Category: Atp-binding]]
-[[Category: Calmodulin-binding]]
-[[Category: Contractile protein]]
-[[Category: Freeze substitution]]
-[[Category: Isometric contraction]]
-[[Category: Methylation]]
-[[Category: Microtomy]]
-[[Category: Motor protein]]
-[[Category: Muscle protein]]