View source for 3qmz


==Crystal structure of the cytoplasmic dynein heavy chain motor domain==
<StructureSection load='3qmz' size='340' side='right'caption='[[3qmz]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qmz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Schistosoma_japonicum Schistosoma japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QMZ 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]] 6&#8491;</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=3qmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmz OCA], [https://pdbe.org/3qmz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qmz RCSB], [https://www.ebi.ac.uk/pdbsum/3qmz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qmz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DYHC_YEAST DYHC_YEAST] 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. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.<ref>PMID:15642746</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dyneins are microtubule-based motor proteins that power ciliary beating, transport intracellular cargos, and help to construct the mitotic spindle. Evolved from ring-shaped hexameric AAA-family adenosine triphosphatases (ATPases), dynein's large size and complexity have posed challenges for understanding its structure and mechanism. Here, we present a 6 angstrom crystal structure of a functional dimer of two ~300-kilodalton motor domains of yeast cytoplasmic dynein. The structure reveals an unusual asymmetric arrangement of ATPase domains in the ring-shaped motor domain, the manner in which the mechanical element interacts with the ATPase ring, and an unexpected interaction between two coiled coils that create a base for the microtubule binding domain. The arrangement of these elements provides clues as to how adenosine triphosphate-driven conformational changes might be transmitted across the motor domain.

Crystal structure of the dynein motor domain.,Carter AP, Cho C, Jin L, Vale RD Science. 2011 Mar 4;331(6021):1159-65. Epub 2011 Feb 17. PMID:21330489<ref>PMID:21330489</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qmz" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dynein 3D structures|Dynein 3D structures]]
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Schistosoma japonicum]]
[[Category: Carter AP]]
[[Category: Cho C]]
[[Category: Jin L]]
[[Category: Vale RD]]