1mne: Difference between revisions
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==TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATE== | ==TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATE== | ||
<StructureSection load='1mne' size='340' side='right' caption='[[1mne]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1mne' size='340' side='right' caption='[[1mne]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Myosin_ATPase Myosin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.1 3.6.4.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Myosin_ATPase Myosin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.1 3.6.4.1] </span></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=1mne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mne OCA], [http://pdbe.org/1mne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mne RCSB], [http://www.ebi.ac.uk/pdbsum/1mne PDBsum]</span></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=1mne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mne OCA], [http://pdbe.org/1mne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mne RCSB], [http://www.ebi.ac.uk/pdbsum/1mne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mne ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mn/1mne_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mn/1mne_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1mne" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1mne" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Atpase]] | [[Category: Atpase]] | ||
[[Category: Coiled coil]] | |||
[[Category: Contractile protein]] | [[Category: Contractile protein]] | ||
[[Category: Heptad repeat pattern]] | [[Category: Heptad repeat pattern]] | ||
Revision as of 10:40, 31 January 2018
TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATETRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATE
Structural highlights
Function[MYS2_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of the magnesium pyrophosphate complex of the truncated head of Dictyostelium myosin has been determined by molecular replacement at 2.7 A resolution and refined to a crystallographic R-factor of 16.0%. The crystals belong to the orthorhombic space group P2(1)2(1)2, where a = 105.2 A, b = 182.1 A, and c = 54.5 A. The conformation of the protein around the magnesium pyrophosphate is very similar to that seen when magnesium ADP-beryllium fluoride binds in the active site. The latter complex mimics the binding of ATP prior to hydrolysis. The pyrophosphate molecule occupies the beta- and gamma-phosphate sites, where the two phosphorus atoms are in the same positions as the beta-phosphate and the BeFx moiety of the beryllium fluoride-trapped ADP. The surrounding active site residues are almost perfectly superimposable in the two structures and the hydrogen-bonding interactions that the PPi makes with the protein are essentially identical. The similarity between the MgPPi and MgADP.BeFx complex with S1Dc suggests that the conformational change, which occurs when ATP binds to actomyosin and which reduces the affinity of myosin for actin, is caused by the binding of the gamma- and beta-phosphate groups of the nucleotide. This then implies that the role of the remainder of the substrate is to increase the binding affinity for myosin and thus to drive the equilibrium toward dissociation of myosin from actin. X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 A resolution.,Smith CA, Rayment I Biochemistry. 1995 Jul 18;34(28):8973-81. PMID:7619796[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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