2w4h
From Proteopedia
(Difference between revisions)
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- | + | ==Isometrically contracting insect asynchronous flight muscle quick frozen after a quick release step== | |
- | + | <StructureSection load='2w4h' size='340' side='right' caption='[[2w4h]], [[Resolution|resolution]] 35.00Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2w4h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W4H FirstGlance]. <br> | |
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i84|1i84]], [[2w4a|2w4a]], [[1mvw|1mvw]], [[1o1a|1o1a]], [[1o1f|1o1f]], [[1o18|1o18]], [[1m8q|1m8q]], [[2w4g|2w4g]], [[1o19|1o19]], [[1alm|1alm]], [[1o1b|1o1b]], [[1o1e|1o1e]], [[1o1c|1o1c]], [[1o1d|1o1d]], [[2mys|2mys]], [[1o1g|1o1g]]</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=2w4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w4h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w4h RCSB], [http://www.ebi.ac.uk/pdbsum/2w4h PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == 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/w4/2w4h_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/chain_selection.php?pdb_ID=2ata 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. | ||
- | + | 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> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
*[[Myosin|Myosin]] | *[[Myosin|Myosin]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
- | [[Category: Franzini-Armstrong, C | + | [[Category: Franzini-Armstrong, C]] |
- | [[Category: Goldman, Y E | + | [[Category: Goldman, Y E]] |
- | [[Category: Liu, J | + | [[Category: Liu, J]] |
- | [[Category: Lucaveche, C | + | [[Category: Lucaveche, C]] |
- | [[Category: Reedy, M C | + | [[Category: Reedy, M C]] |
- | [[Category: Reedy, M K | + | [[Category: Reedy, M K]] |
- | [[Category: Sasaki, H | + | [[Category: Sasaki, H]] |
- | [[Category: Taylor, K A | + | [[Category: Taylor, K A]] |
- | [[Category: Tregear, R T | + | [[Category: Tregear, R T]] |
- | [[Category: Winkler, H | + | [[Category: Winkler, H]] |
- | [[Category: Wu, S | + | [[Category: Wu, S]] |
[[Category: Actin-binding]] | [[Category: Actin-binding]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] |
Revision as of 14:04, 17 December 2014
Isometrically contracting insect asynchronous flight muscle quick frozen after a quick release step
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Categories: Gallus gallus | Franzini-Armstrong, C | Goldman, Y E | Liu, J | Lucaveche, C | Reedy, M C | Reedy, M K | Sasaki, H | Taylor, K A | Tregear, R T | Winkler, H | Wu, S | Actin-binding | Atp-binding | Calmodulin-binding | Contractile protein | Freeze substitution | Isometric contraction | Methylation | Microtomy | Motor protein | Muscle protein