2w4v: Difference between revisions
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==Isometrically contracting insect asynchronous flight muscle quick frozen after a quick release step== | |||
<StructureSection load='2w4v' size='340' side='right' caption='[[2w4v]], [[Resolution|resolution]] 35.00Å' scene=''> | |||
=== | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2w4v]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W4V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W4V FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2w4t|2w4t]], [[1sr6|1sr6]], [[1s5g|1s5g]], [[1kqm|1kqm]], [[1qvi|1qvi]], [[1kwo|1kwo]], [[1dfl|1dfl]], [[1scm|1scm]], [[1b7t|1b7t]], [[1wdc|1wdc]], [[1l2o|1l2o]], [[1kk7|1kk7]], [[1dfk|1dfk]], [[1kk8|1kk8]]</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=2w4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w4v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w4v RCSB], [http://www.ebi.ac.uk/pdbsum/2w4v 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/w4/2w4v_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: Argopecten irradians]] | [[Category: Argopecten irradians]] | ||
[[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: Contractile protein]] | [[Category: Contractile protein]] | ||
