5w3f

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<SX load='5w3f' size='340' side='right' viewer='molstar' caption='[[5w3f]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<SX load='5w3f' size='340' side='right' viewer='molstar' caption='[[5w3f]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5w3f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W3F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5W3F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5w3f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W3F 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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3.7&#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=5w3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w3f OCA], [http://pdbe.org/5w3f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w3f RCSB], [http://www.ebi.ac.uk/pdbsum/5w3f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w3f 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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5w3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w3f OCA], [https://pdbe.org/5w3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w3f RCSB], [https://www.ebi.ac.uk/pdbsum/5w3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w3f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TBA1_YEAST TBA1_YEAST]] 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/TBB_YEAST TBB_YEAST]] 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/TBA1_YEAST TBA1_YEAST] 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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Microtubules are polymers of alphabeta-tubulin heterodimers essential for all eukaryotes. Despite sequence conservation, there are significant structural differences between microtubules assembled in vitro from mammalian or budding yeast tubulin. Yeast MTs were not observed to undergo compaction at the interdimer interface as seen for mammalian microtubules upon GTP hydrolysis. Lack of compaction might reflect slower GTP hydrolysis or a different degree of allosteric coupling in the lattice. The microtubule plus end-tracking protein Bim1 binds yeast microtubules both between alphabeta-tubulin heterodimers, as seen for other organisms, and within tubulin dimers, but binds mammalian tubulin only at interdimer contacts. At the concentrations used in cryo-electron microscopy, Bim1 causes the compaction of yeast microtubules and induces their rapid disassembly. Our studies demonstrate structural differences between yeast and mammalian microtubules that likely underlie their differing polymerization dynamics. These differences may reflect adaptations to the demands of different cell size or range of physiological growth temperatures.
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Structural differences between yeast and mammalian microtubules revealed by cryo-EM.,Howes SC, Geyer EA, LaFrance B, Zhang R, Kellogg EH, Westermann S, Rice LM, Nogales E J Cell Biol. 2017 Sep 4;216(9):2669-2677. doi: 10.1083/jcb.201612195. Epub 2017, Jun 26. PMID:28652389<ref>PMID:28652389</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 5w3f" 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/>
 
__TOC__
__TOC__
</SX>
</SX>
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[[Category: Baker's yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Geyer, E A]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Howes, S C]]
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[[Category: Geyer EA]]
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[[Category: Kellogg, E H]]
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[[Category: Howes SC]]
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[[Category: LaFrance, B]]
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[[Category: Kellogg EH]]
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[[Category: Nogales, E]]
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[[Category: LaFrance B]]
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[[Category: Rice, L M]]
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[[Category: Nogales E]]
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[[Category: Westermann, S]]
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[[Category: Rice LM]]
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[[Category: Zhang, R]]
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[[Category: Westermann S]]
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[[Category: Cytoskeleton]]
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[[Category: Zhang R]]
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[[Category: Hydrolase]]
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[[Category: Tubulin]]
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Current revision

Yeast tubulin polymerized with GTP in vitro

5w3f, resolution 3.70Å

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OCA

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