|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5afr' size='340' side='right'caption='[[5afr]], [[Resolution|resolution]] 5.00Å' scene=''> | | <StructureSection load='5afr' size='340' side='right'caption='[[5afr]], [[Resolution|resolution]] 5.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5afr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AFR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5afr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AFR FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5afr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afr OCA], [http://pdbe.org/5afr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5afr RCSB], [http://www.ebi.ac.uk/pdbsum/5afr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5afr ProSAT]</span></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=5afr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afr OCA], [https://pdbe.org/5afr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5afr RCSB], [https://www.ebi.ac.uk/pdbsum/5afr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5afr 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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carter, A P]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Diamant, A G]] | + | [[Category: Carter AP]] |
| - | [[Category: Motz, C]] | + | [[Category: Diamant AG]] |
| - | [[Category: Patel, N A]] | + | [[Category: Motz C]] |
| - | [[Category: Robinson, C V]] | + | [[Category: Patel NA]] |
| - | [[Category: Schlager, M A]] | + | [[Category: Robinson CV]] |
| - | [[Category: Urnavicius, L]] | + | [[Category: Schlager MA]] |
| - | [[Category: Yu, M]] | + | [[Category: Urnavicius L]] |
| - | [[Category: Zhang, K]] | + | [[Category: Yu M]] |
| - | [[Category: Dynein]]
| + | [[Category: Zhang K]] |
| - | [[Category: Heavy chain]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Tail]]
| + | |
| 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]
Publication Abstract from PubMed
Dynactin is an essential cofactor for the microtubule motor cytoplasmic dynein-1. We report the structure of the 23-subunit dynactin complex by cryo-electron microscopy to 4.0 angstroms. Our reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of beta-actin. The filament is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the alpha-helical shoulder domain. A further 8.2 angstrom structure of the complex between dynein, dynactin, and the motility-inducing cargo adaptor Bicaudal-D2 shows how the translational symmetry of the dynein tail matches that of the dynactin filament. The Bicaudal-D2 coiled coil runs between dynein and dynactin to stabilize the mutually dependent interactions between all three components.
The structure of the dynactin complex and its interaction with dynein.,Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP Science. 2015 Mar 27;347(6229):1441-6. doi: 10.1126/science.aaa4080. Epub 2015, Feb 12. PMID:25814576[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
- ↑ Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP. The structure of the dynactin complex and its interaction with dynein. Science. 2015 Mar 27;347(6229):1441-6. doi: 10.1126/science.aaa4080. Epub 2015, Feb 12. PMID:25814576 doi:http://dx.doi.org/10.1126/science.aaa4080
|
