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3vkg

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==X-ray structure of an MTBD truncation mutant of dynein motor domain==
==X-ray structure of an MTBD truncation mutant of dynein motor domain==
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<StructureSection load='3vkg' size='340' side='right' caption='[[3vkg]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
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<StructureSection load='3vkg' size='340' side='right'caption='[[3vkg]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vkg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VKG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vkg]] 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=3VKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VKG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.81&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ay1|3ay1]], [[3vkh|3vkh]]</td></tr>
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<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>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB_G0276355, dhcA, slime mold ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32630 synthetic construct])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vkg OCA], [https://pdbe.org/3vkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vkg RCSB], [https://www.ebi.ac.uk/pdbsum/3vkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vkg ProSAT]</span></td></tr>
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<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=3vkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vkg RCSB], [http://www.ebi.ac.uk/pdbsum/3vkg PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/DYHC_DICDI DYHC_DICDI] Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.
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Dyneins are microtubule-based AAA(+) motor complexes that power ciliary beating, cell division, cell migration and intracellular transport. Here we report the most complete structure obtained so far, to our knowledge, of the 380-kDa motor domain of Dictyostelium discoideum cytoplasmic dynein at 2.8 A resolution; the data are reliable enough to discuss the structure and mechanism at the level of individual amino acid residues. Features that can be clearly visualized at this resolution include the coordination of ADP in each of four distinct nucleotide-binding sites in the ring-shaped AAA(+) ATPase unit, a newly identified interaction interface between the ring and mechanical linker, and junctional structures between the ring and microtubule-binding stalk, all of which should be critical for the mechanism of dynein motility. We also identify a long-range allosteric communication pathway between the primary ATPase and the microtubule-binding sites. Our work provides a framework for understanding the mechanism of dynein-based motility.
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The 2.8 A crystal structure of the dynein motor domain.,Kon T, Oyama T, Shimo-Kon R, Imamula K, Shima T, Sutoh K, Kurisu G Nature. 2012 Mar 7;484(7394):345-50. doi: 10.1038/nature10955. PMID:22398446<ref>PMID:22398446</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Dynein|Dynein]]
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*[[Dynein 3D structures|Dynein 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Synthetic construct]]
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[[Category: Dictyostelium discoideum]]
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[[Category: Kon, T]]
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[[Category: Large Structures]]
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[[Category: Kurisu, G]]
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[[Category: Kon T]]
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[[Category: Oyama, T]]
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[[Category: Kurisu G]]
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[[Category: Shimo-Kon, R]]
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[[Category: Oyama T]]
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[[Category: Suto, K]]
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[[Category: Shimo-Kon R]]
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[[Category: Aaa+ protein]]
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[[Category: Suto K]]
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[[Category: Microtuble]]
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[[Category: Molecular motor]]
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[[Category: Motor protein]]
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Current revision

X-ray structure of an MTBD truncation mutant of dynein motor domain

PDB ID 3vkg

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