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2w4w

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Revision as of 10:37, 12 January 2022

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

2w4w, resolution 35.00Å

Structural highlights

2w4w is a 3 chain structure with sequence from Argopecten irradians. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2w4t, 1sr6, 1s5g, 1kqm, 1qvi, 1kwo, 1dfl, 1scm, 1b7t, 1wdc, 1l2o, 1kk7, 1dfk, 1kk8
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYS_ARGIR] Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. [MLE_ARGIR] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity. [MLR_ARGIR] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity.

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. Structural Changes in Isometrically Contracting Insect Flight Muscle Trapped following a Mechanical Perturbation. PLoS One. 2012;7(6):e39422. Epub 2012 Jun 25. PMID:22761792 doi:10.1371/journal.pone.0039422

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2w4w"

@@ Line 3: / Line 3: @@
 <SX load='2w4w' size='340' side='right' viewer='molstar' caption='[[2w4w]], [[Resolution|resolution]] 35.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2w4w]] 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=2W4W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2W4W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2w4w]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W4W 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>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[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]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2w4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w4w OCA], [http://pdbe.org/2w4w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w4w RCSB], [http://www.ebi.ac.uk/pdbsum/2w4w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w4w ProSAT]</span></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=2w4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w4w OCA], [https://pdbe.org/2w4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w4w RCSB], [https://www.ebi.ac.uk/pdbsum/2w4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w4w ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYS_ARGIR MYS_ARGIR]] Muscle contraction.  Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. [[http://www.uniprot.org/uniprot/MLE_ARGIR MLE_ARGIR]] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity. [[http://www.uniprot.org/uniprot/MLR_ARGIR MLR_ARGIR]] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity.
+[[https://www.uniprot.org/uniprot/MYS_ARGIR MYS_ARGIR]] Muscle contraction.  Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. [[https://www.uniprot.org/uniprot/MLE_ARGIR MLE_ARGIR]] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity. [[https://www.uniprot.org/uniprot/MLR_ARGIR MLR_ARGIR]] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2w4w

From Proteopedia

Revision as of 10:37, 12 January 2022

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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