1mne: Difference between revisions

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-[[Image:1mne.gif|left|200px]]<br /><applet load="1mne" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1mne, resolution 2.7&Aring;" />
-'''TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATE'''<br />
-==Overview==
+==TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATE==
-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.
+<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 [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='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='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'>[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 ==
+[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]]
+Check<jmol>
+  <jmolCheckbox>
+    <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>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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>
-==About this Structure==
+==See Also==
-MNE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with MG and POP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MNE OCA].
+*[[Myosin 3D Structures|Myosin 3D Structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7619796 7619796]
 [[Category: Dictyostelium discoideum]]
-[[Category: Myosin ATPase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Rayment I]]
-[[Category: Rayment, I.]]
+[[Category: Smith CA]]
-[[Category: Smith, C.A.]]
-[[Category: MG]]
-[[Category: POP]]
-[[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]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:33:04 2007''