1g8x: Difference between revisions

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 <StructureSection load='1g8x' size='340' side='right'caption='[[1g8x]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1g8x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G8X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1g8x]] 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=1G8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G8X FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1g8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g8x OCA], [https://pdbe.org/1g8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g8x RCSB], [https://www.ebi.ac.uk/pdbsum/1g8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g8x 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.
+[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.[https://www.uniprot.org/uniprot/ACTNA_DICDI ACTNA_DICDI] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin network in the cortical cytoskeleton.<ref>PMID:10411959</ref> <ref>PMID:10413681</ref> <ref>PMID:10704840</ref> <ref>PMID:1732064</ref> <ref>PMID:3956480</ref> <ref>PMID:6746725</ref> <ref>PMID:8486739</ref> <ref>PMID:8937986</ref>
 == 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=1g8x ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the nucleotide-binding region into force-generating movements of larger protein domains. We present the 2.8 A resolution crystal structure of an artificial actin-based motor. By combining the catalytic domain of myosin II with a 130 A conformational amplifier consisting of repeats 1 and 2 of alpha-actinin, we demonstrate that it is possible to genetically engineer single-polypeptide molecular motors with precisely defined lever arm lengths and specific motile properties. Furthermore, our structure shows the consequences of mutating a conserved salt bridge in the nucleotide-binding region. Disruption of this salt bridge, which is known to severely inhibit ATP hydrolysis activity, appears to interfere with formation of myosin's catalytically active 'closed' conformation. Finally, we describe the structure of alpha-actinin repeats 1 and 2 as being composed of two rigid, triple-helical bundles linked by an uninterrupted alpha-helix. This fold is very similar to the previously described structures of alpha-actinin repeats 2 and 3, and alpha-spectrin repeats 16 and 17.
-Structure of a genetically engineered molecular motor.,Kliche W, Fujita-Becker S, Kollmar M, Manstein DJ, Kull FJ EMBO J. 2001 Jan 15;20(1-2):40-6. PMID:11226153<ref>PMID:11226153</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1g8x" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 28: @@
 __TOC__
 </StructureSection>
-[[Category: Dicdi]]
+[[Category: Dictyostelium discoideum]]
 [[Category: Large Structures]]
-[[Category: Fujita-Becker, S]]
+[[Category: Fujita-Becker S]]
-[[Category: Kliche, W]]
+[[Category: Kliche W]]
-[[Category: Kollmar, M]]
+[[Category: Kollmar M]]
-[[Category: Kull, F J]]
+[[Category: Kull FJ]]
-[[Category: Manstein, D J]]
+[[Category: Manstein DJ]]
-[[Category: Alpha-actinin]]
-[[Category: Dictyostelium]]
-[[Category: Lever arm]]
-[[Category: Motor]]
-[[Category: Myosin]]
-[[Category: Protein engineering]]
-[[Category: Structural protein]]