3jax

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==Heavy meromyosin from Schistosoma mansoni muscle thick filament by negative stain EM==
==Heavy meromyosin from Schistosoma mansoni muscle thick filament by negative stain EM==
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<StructureSection load='3jax' size='340' side='right' caption='[[3jax]], [[Resolution|resolution]] 23.00&Aring;' scene=''>
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<SX load='3jax' size='340' side='right' viewer='molstar' caption='[[3jax]], [[Resolution|resolution]] 23.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3jax]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JAX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3jax]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JAX FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dtp|3dtp]], [[1i84|1i84]], [[2fxm|2fxm]], [[1b7t|1b7t]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 23&#8491;</td></tr>
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<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=3jax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jax OCA], [http://pdbe.org/3jax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jax RCSB], [http://www.ebi.ac.uk/pdbsum/3jax PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jax OCA], [https://pdbe.org/3jax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jax RCSB], [https://www.ebi.ac.uk/pdbsum/3jax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jax ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0R4I956_SCHMA A0A0R4I956_SCHMA]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Muscle contraction involves the interaction of the myosin heads of the thick filaments with actin subunits of the thin filaments. Relaxation occurs when this interaction is blocked by molecular switches on these filaments. In many muscles, myosin-linked regulation involves phosphorylation of the myosin regulatory light chains (RLCs). Electron microscopy of vertebrate smooth muscle myosin molecules (regulated by phosphorylation) has provided insight into the relaxed structure, revealing that myosin is switched off by intramolecular interactions between its two heads, the free head and the blocked head. Three-dimensional reconstruction of frozen-hydrated specimens revealed that this asymmetric head interaction is also present in native thick filaments of tarantula striated muscle. Our goal in this study was to elucidate the structural features of the tarantula filament involved in phosphorylation-based regulation. A new reconstruction revealed intra- and intermolecular myosin interactions in addition to those seen previously. To help interpret the interactions, we sequenced the tarantula RLC and fitted an atomic model of the myosin head that included the predicted RLC atomic structure and an S2 (subfragment 2) crystal structure to the reconstruction. The fitting suggests one intramolecular interaction, between the cardiomyopathy loop of the free head and its own S2, and two intermolecular interactions, between the cardiac loop of the free head and the essential light chain of the blocked head and between the Leu305-Gln327 interaction loop of the free head and the N-terminal fragment of the RLC of the blocked head. These interactions, added to those previously described, would help switch off the thick filament. Molecular dynamics simulations suggest how phosphorylation could increase the helical content of the RLC N-terminus, weakening these interactions, thus releasing both heads and activating the thick filament.
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Muscle tissues are classically divided into two major types, depending on the presence or absence of striations. In striated muscles, the actin filaments are anchored at Z-lines and the myosin and actin filaments are in register, whereas in smooth muscles, the actin filaments are attached to dense bodies and the myosin and actin filaments are out of register. The structure of the filaments in smooth muscles is also different from that in striated muscles. Here we have studied the structure of myosin filaments from the smooth muscles of the human parasite Schistosoma mansoni. We find, surprisingly, that they are indistinguishable from those in an arthropod striated muscle. This structural similarity is supported by sequence comparison between the schistosome myosin II heavy chain and known striated muscle myosins. In contrast, the actin filaments of schistosomes are similar to those of smooth muscles, lacking troponin-dependent regulation. We conclude that schistosome muscles are hybrids, containing striated muscle-like myosin filaments and smooth muscle-like actin filaments in a smooth muscle architecture. This surprising finding has broad significance for understanding how muscles are built and how they evolved, and challenges the paradigm that smooth and striated muscles always have distinctly different components.
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Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity.,Alamo L, Wriggers W, Pinto A, Bartoli F, Salazar L, Zhao FQ, Craig R, Padron R J Mol Biol. 2008 Dec 26;384(4):780-97. Epub 2008 Oct 14. PMID:18951904<ref>PMID:18951904</ref>
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An invertebrate smooth muscle with striated muscle myosin filaments.,Sulbaran G, Alamo L, Pinto A, Marquez G, Mendez F, Padron R, Craig R Proc Natl Acad Sci U S A. 2015 Oct 6. pii: 201513439. PMID:26443857<ref>PMID:26443857</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Large Structures]]
[[Category: Schistosoma mansoni]]
[[Category: Schistosoma mansoni]]
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[[Category: Alamo, L]]
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[[Category: Alamo L]]
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[[Category: Craig, R]]
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[[Category: Craig R]]
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[[Category: Marquez, G]]
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[[Category: Marquez G]]
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[[Category: Mendez, F]]
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[[Category: Mendez F]]
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[[Category: Padron, R]]
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[[Category: Padron R]]
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[[Category: Pinto, A]]
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[[Category: Pinto A]]
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[[Category: Sulbaran, G]]
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[[Category: Sulbaran G]]
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[[Category: Coiled-coil]]
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[[Category: Contractile protein]]
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[[Category: Essential light chain]]
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[[Category: Heavy meromyosin]]
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[[Category: Motor protein]]
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[[Category: Muscle protein]]
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[[Category: Myosin subfragment 2]]
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[[Category: Regulatory light chain]]
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[[Category: Smooth muscle]]
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Current revision

Heavy meromyosin from Schistosoma mansoni muscle thick filament by negative stain EM

3jax, resolution 23.00Å

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