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5h53

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The structure of rabbit skeletal muscle actomyosin rigor complex at 5.2 angstrom.

5h53, resolution 5.20Å

Structural highlights

5h53 is a 5 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 5.2Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9GJP9_RABIT

Publication Abstract from PubMed

Muscle contraction is driven by cyclic association and dissociation of myosin head of the thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin. However, because of the absence of actomyosin rigour structure at high resolution, it still remains unclear how the strong binding of myosin to actin filament triggers the release of hydrolysis products and how ATP binding causes their dissociation. Here we report the structure of mammalian skeletal muscle actomyosin rigour complex at 5.2 A resolution by electron cryomicroscopy. Comparison with the structures of myosin in various states shows a distinctly large conformational change, providing insights into the ATPase-coupled reaction cycle of actomyosin. Based on our observations, we hypothesize that asymmetric binding along the actin filament could function as a Brownian ratchet by favouring directionally biased thermal motions of myosin and actin.

Structure of actomyosin rigour complex at 5.2 A resolution and insights into the ATPase cycle mechanism.,Fujii T, Namba K Nat Commun. 2017 Jan 9;8:13969. doi: 10.1038/ncomms13969. PMID:28067235^[1]

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

References

↑ Fujii T, Namba K. Structure of actomyosin rigour complex at 5.2 A resolution and insights into the ATPase cycle mechanism. Nat Commun. 2017 Jan 9;8:13969. doi: 10.1038/ncomms13969. PMID:28067235 doi:http://dx.doi.org/10.1038/ncomms13969

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5h53"

Categories: Large Structures | Oryctolagus cuniculus | Fujii T | Namba K

@@ Line 3: / Line 3: @@
 <SX load='5h53' size='340' side='right' viewer='molstar' caption='[[5h53]], [[Resolution|resolution]] 5.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5h53]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H53 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5h53]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H53 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.2&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></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=5h53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h53 OCA], [http://pdbe.org/5h53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h53 RCSB], [http://www.ebi.ac.uk/pdbsum/5h53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h53 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=5h53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h53 OCA], [https://pdbe.org/5h53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h53 RCSB], [https://www.ebi.ac.uk/pdbsum/5h53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h53 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/MYL1_RABIT MYL1_RABIT]] Regulatory light chain of myosin. Does not bind calcium.
+[https://www.uniprot.org/uniprot/Q9GJP9_RABIT Q9GJP9_RABIT]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 29: / Line 29: @@
 [[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Fujii, T]]
+[[Category: Fujii T]]
-[[Category: Namba, K]]
+[[Category: Namba K]]
-[[Category: Actin]]
-[[Category: Motor protein]]
-[[Category: Muscle]]
-[[Category: Myosin]]
-[[Category: Rigor complex]]

5h53

From Proteopedia

Current revision

The structure of rabbit skeletal muscle actomyosin rigor complex at 5.2 angstrom.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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