3j67

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<SX load='3j67' size='340' side='right' viewer='molstar' caption='[[3j67]], [[Resolution|resolution]] 34.00&Aring;' scene=''>
<SX load='3j67' size='340' side='right' viewer='molstar' caption='[[3j67]], [[Resolution|resolution]] 34.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3j67]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strongylocentrotus_purpuratus Strongylocentrotus purpuratus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J67 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3j67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strongylocentrotus_purpuratus Strongylocentrotus purpuratus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J67 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4aki|4aki]], [[3j68|3j68]]</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">Electron Microscopy, [[Resolution|Resolution]] 34&#8491;</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=3j67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j67 OCA], [http://pdbe.org/3j67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j67 RCSB], [http://www.ebi.ac.uk/pdbsum/3j67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j67 ProSAT]</span></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=3j67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j67 OCA], [https://pdbe.org/3j67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j67 RCSB], [https://www.ebi.ac.uk/pdbsum/3j67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j67 ProSAT]</span></td></tr>
</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_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>
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Dyneins are large microtubule motor proteins required for mitosis, intracellular transport and ciliary and flagellar motility. They generate force through a power-stroke mechanism, which is an ATP-consuming cycle of pre- and post-power-stroke conformational changes that cause relative motion between different dynein domains. However, key structural details of dynein's force generation remain elusive. Here, using cryo-electron tomography of intact, active (that is, beating), rapidly frozen sea urchin sperm flagella, we determined the in situ three-dimensional structures of all domains of both pre- and post-power-stroke dynein, including the previously unresolved linker and stalk of pre-power-stroke dynein. Our results reveal that the rotation of the head relative to the linker is the key action in dynein movement, and that there are at least two distinct pre-power-stroke conformations: pre-I (microtubule-detached) and pre-II (microtubule-bound). We provide three-dimensional reconstructions of native dyneins in three conformational states, in situ, allowing us to propose a molecular model of the structural cycle underlying dynein movement.
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Structural mechanism of the dynein power stroke.,Lin J, Okada K, Raytchev M, Smith MC, Nicastro D Nat Cell Biol. 2014 Apr 13. doi: 10.1038/ncb2939. PMID:24727830<ref>PMID:24727830</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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<div class="pdbe-citations 3j67" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Strongylocentrotus purpuratus]]
[[Category: Strongylocentrotus purpuratus]]
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[[Category: Lin, J]]
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[[Category: Lin J]]
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[[Category: Nicastro, D]]
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[[Category: Nicastro D]]
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[[Category: Okada, K]]
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[[Category: Okada K]]
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[[Category: Raytchev, M]]
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[[Category: Raytchev M]]
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[[Category: Smith, M C]]
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[[Category: Smith MC]]
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[[Category: Motor protein]]
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Current revision

Structural mechanism of the dynein powerstroke (post-powerstroke state)

3j67, resolution 34.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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