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| | <StructureSection load='6z7t' size='340' side='right'caption='[[6z7t]], [[Resolution|resolution]] 1.88Å' scene=''> | | <StructureSection load='6z7t' size='340' side='right'caption='[[6z7t]], [[Resolution|resolution]] 1.88Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6z7t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z7T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Z7T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6z7t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z7T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mhcA, DDB_G0286355 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 DICDI])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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=6z7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z7t OCA], [http://pdbe.org/6z7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6z7t RCSB], [http://www.ebi.ac.uk/pdbsum/6z7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6z7t 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=6z7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z7t OCA], [https://pdbe.org/6z7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z7t RCSB], [https://www.ebi.ac.uk/pdbsum/6z7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z7t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYS2_DICDI MYS2_DICDI]] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. | + | [https://www.uniprot.org/uniprot/MYS2_DICDI MYS2_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6z7t" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6z7t" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Myosin 3D Structures|Myosin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dicdi]] | + | [[Category: Dictyostelium discoideum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ewert, W]] | + | [[Category: Ewert W]] |
| - | [[Category: Preller, M]] | + | [[Category: Preller M]] |
| - | [[Category: Adp-release]]
| + | |
| - | [[Category: Blebbistatin]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Motorprotein]]
| + | |
| - | [[Category: Myosin]]
| + | |
| Structural highlights
6z7t is a 2 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.88Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MYS2_DICDI Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.
Publication Abstract from PubMed
The motor protein myosin drives a wide range of cellular and muscular functions by generating directed movement and force, fueled through adenosine triphosphate (ATP) hydrolysis. Release of the hydrolysis product adenosine diphosphate (ADP) is a fundamental and regulatory process during force production. However, details about the molecular mechanism accompanying ADP release are scarce due to the lack of representative structures. Here we solved a novel blebbistatin-bound myosin conformation with critical structural elements in positions between the myosin pre-power stroke and rigor states. ADP in this structure is repositioned towards the surface by the phosphate-sensing P-loop, and stabilized in a partially unbound conformation via a salt-bridge between Arg131 and Glu187. A 5 A rotation separates the mechanical converter in this conformation from the rigor position. The crystallized myosin structure thus resembles a conformation towards the end of the two-step power stroke, associated with ADP release. Computationally reconstructing ADP release from myosin by means of molecular dynamics simulations further supported the existence of an equivalent conformation along the power stroke that shows the same major characteristics in the myosin motor domain as the resolved blebbistatin-bound myosin-II.ADP crystal structure, and identified a communication hub centered on Arg232 that mediates chemomechanical energy transduction.
Structural and Computational Insights into a Blebbistatin-Bound Myosin*ADP Complex with Characteristics of an ADP-Release Conformation along the Two-Step Myosin Power Stoke.,Ewert W, Franz P, Tsiavaliaris G, Preller M Int J Mol Sci. 2020 Oct 8;21(19). pii: ijms21197417. doi: 10.3390/ijms21197417. PMID:33049993[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ewert W, Franz P, Tsiavaliaris G, Preller M. Structural and Computational Insights into a Blebbistatin-Bound Myosin*ADP Complex with Characteristics of an ADP-Release Conformation along the Two-Step Myosin Power Stoke. Int J Mol Sci. 2020 Oct 8;21(19). pii: ijms21197417. doi: 10.3390/ijms21197417. PMID:33049993 doi:http://dx.doi.org/10.3390/ijms21197417
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