6e88

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<SX load='6e88' size='340' side='right' viewer='molstar' caption='[[6e88]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
<SX load='6e88' size='340' side='right' viewer='molstar' caption='[[6e88]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6e88]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E88 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6E88 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6e88]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E88 FirstGlance]. <br>
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</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></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]] 4.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6e88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e88 OCA], [http://pdbe.org/6e88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e88 RCSB], [http://www.ebi.ac.uk/pdbsum/6e88 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e88 ProSAT]</span></td></tr>
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<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></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=6e88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e88 OCA], [https://pdbe.org/6e88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e88 RCSB], [https://www.ebi.ac.uk/pdbsum/6e88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e88 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TBA2_CAEEL TBA2_CAEEL]] 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. [[http://www.uniprot.org/uniprot/TBB2_CAEEL TBB2_CAEEL]] 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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[https://www.uniprot.org/uniprot/TBA2_CAEEL TBA2_CAEEL] 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The dynamic instability of microtubules is a conserved and fundamental mechanism in eukaryotes. Yet microtubules from different species diverge in their growth rates, lattice structures, and responses to GTP hydrolysis. Therefore, we do not know what limits microtubule growth, what determines microtubule structure, or whether the mechanisms of dynamic instability are universal. Here, we studied microtubules from the nematode C. elegans, which have strikingly fast growth rates and non-canonical lattices in vivo. Using a reconstitution approach, we discovered that C. elegans microtubules combine intrinsically fast growth with very frequent catastrophes. We solved the structure of C. elegans microtubules to 4.8 A and discovered sequence divergence in the lateral contact loops, one of which is ordered in C. elegans but unresolved in other species. We provide direct evidence that C. elegans tubulin has a higher free energy in solution and propose a model wherein the ordering of lateral contact loops activates tubulin for growth.
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The Structure and Dynamics of C. elegans Tubulin Reveals the Mechanistic Basis of Microtubule Growth.,Chaaban S, Jariwala S, Hsu CT, Redemann S, Kollman JM, Muller-Reichert T, Sept D, Bui KH, Brouhard GJ Dev Cell. 2018 Sep 18. pii: S1534-5807(18)30696-8. doi:, 10.1016/j.devcel.2018.08.023. PMID:30245157<ref>PMID:30245157</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 6e88" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
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== References ==
 
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<references/>
 
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__TOC__
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[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brouhard, G J]]
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[[Category: Brouhard GJ]]
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[[Category: Bui, K H]]
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[[Category: Bui KH]]
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[[Category: Chaaban, S]]
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[[Category: Chaaban S]]
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[[Category: Chieh-Ting, H]]
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[[Category: Chieh-Ting H]]
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[[Category: Jariwala, S]]
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[[Category: Jariwala S]]
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[[Category: Kollman, J]]
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[[Category: Kollman J]]
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[[Category: Muller-Reichert, T]]
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[[Category: Muller-Reichert T]]
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[[Category: Redemann, S]]
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[[Category: Redemann S]]
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[[Category: Sept, D]]
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[[Category: Sept D]]
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[[Category: Cytoskeletal protein]]
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[[Category: Structural protein]]
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Current revision

Cryo-EM structure of C. elegans GDP-microtubule

6e88, resolution 4.80Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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