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| | ==Crystal structure of the cytoplasmic dynein heavy chain motor domain== | | ==Crystal structure of the cytoplasmic dynein heavy chain motor domain== |
| - | <StructureSection load='3qmz' size='340' side='right' caption='[[3qmz]], [[Resolution|resolution]] 6.00Å' scene=''> | + | <StructureSection load='3qmz' size='340' side='right'caption='[[3qmz]], [[Resolution|resolution]] 6.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qmz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QMZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qmz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [https://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. 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='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=3qmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmz OCA], [http://pdbe.org/3qmz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qmz RCSB], [http://www.ebi.ac.uk/pdbsum/3qmz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qmz ProSAT]</span></td></tr> | + | </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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> [[http://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. | + | [[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> [[https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Dynein|Dynein]] | + | *[[Dynein 3D structures|Dynein 3D structures]] |
| - | *[[Glutathione S-transferase|Glutathione S-transferase]] | + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Atcc 18824]] | | [[Category: Atcc 18824]] |
| | [[Category: Blood fluke]] | | [[Category: Blood fluke]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Carter, A P]] | | [[Category: Carter, A P]] |
| | [[Category: Cho, C]] | | [[Category: Cho, C]] |
| Structural highlights
Function
[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.[1] [GST26_SCHJA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee WL, Kaiser MA, Cooper JA. The offloading model for dynein function: differential function of motor subunits. J Cell Biol. 2005 Jan 17;168(2):201-7. Epub 2005 Jan 10. PMID:15642746 doi:http://dx.doi.org/10.1083/jcb.200407036
- ↑ Carter AP, Cho C, Jin L, Vale RD. Crystal structure of the dynein motor domain. Science. 2011 Mar 4;331(6021):1159-65. Epub 2011 Feb 17. PMID:21330489 doi:10.1126/science.1202393
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