View source for 6rzb


==Cryo-EM structure of mouse cytoplasmic dynein-1 microtubule binding domain bound to microtubules==
<SX load='6rzb' size='340' side='right' viewer='molstar' caption='[[6rzb]], [[Resolution|resolution]] 5.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rzb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RZB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene></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=6rzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rzb OCA], [https://pdbe.org/6rzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rzb RCSB], [https://www.ebi.ac.uk/pdbsum/6rzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rzb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TBA1B_PIG TBA1B_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
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== Publication Abstract from PubMed ==
Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind microtubules at near atomic resolution. We decorated microtubules with MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7 and determined their cryo-EM structures using helical Relion. The majority of the MTBD is rigid upon binding, with the transition to the high-affinity state controlled by the movement of a single helix at the MTBD interface. DNAH7 contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament. Unexpectedly, we observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. This raises the possibility that dynein coordination in axonemes is mediated via conformational changes in the microtubule.

Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule.,Lacey SE, He S, Scheres SH, Carter AP Elife. 2019 Jul 2;8. pii: 47145. doi: 10.7554/eLife.47145. PMID:31264960<ref>PMID:31264960</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6rzb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dynein 3D structures|Dynein 3D structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Sus scrofa]]
[[Category: Carter AP]]
[[Category: He S]]
[[Category: Lacey SE]]
[[Category: Scheres SHW]]