1mne: Difference between revisions

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 <StructureSection load='1mne' size='340' side='right'caption='[[1mne]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mne]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MNE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mne]] is a 1 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=1MNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MNE FirstGlance]. <br>
-</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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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=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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mne OCA], [https://pdbe.org/1mne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mne RCSB], [https://www.ebi.ac.uk/pdbsum/1mne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mne ProSAT]</span></td></tr>
 </table>
 == 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mne ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The 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<ref>PMID:7619796</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mne" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Myosin 3D Structures|Myosin 3D Structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 11735]]
+[[Category: Dictyostelium discoideum]]
 [[Category: Large Structures]]
-[[Category: Myosin ATPase]]
+[[Category: Rayment I]]
-[[Category: Rayment, I]]
+[[Category: Smith CA]]
-[[Category: Smith, C A]]
-[[Category: Actin-binding]]
-[[Category: Alkylation]]
-[[Category: Atp-binding]]
-[[Category: Atpase]]
-[[Category: Coiled coil]]
-[[Category: Contractile protein]]
-[[Category: Heptad repeat pattern]]
-[[Category: Methylation]]
-[[Category: Myosin]]
-[[Category: Phosphorylation]]