3jaw

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3jaw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JAW FirstGlance]. <br>
<table><tr><td colspan='2'>[[3jaw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JAW 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=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</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]] 3.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3jak|3jak]], [[3jal|3jal]], [[3jar|3jar]], [[3jas|3jas]], [[3jat|3jat]]</div></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=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3jaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jaw OCA], [https://pdbe.org/3jaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jaw RCSB], [https://www.ebi.ac.uk/pdbsum/3jaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jaw 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=3jaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jaw OCA], [https://pdbe.org/3jaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jaw RCSB], [https://www.ebi.ac.uk/pdbsum/3jaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jaw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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. [[https://www.uniprot.org/uniprot/TBB_PIG TBB_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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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Microtubule (MT) dynamic instability is driven by GTP hydrolysis and regulated by microtubule-associated proteins, including the plus-end tracking end-binding protein (EB) family. We report six cryo-electron microscopy (cryo-EM) structures of MTs, at 3.5 A or better resolution, bound to GMPCPP, GTPgammaS, or GDP, either decorated with kinesin motor domain after polymerization or copolymerized with EB3. Subtle changes around the E-site nucleotide during hydrolysis trigger conformational changes in alpha-tubulin around an "anchor point," leading to global lattice rearrangements and strain generation. Unlike the extended lattice of the GMPCPP-MT, the EB3-bound GTPgammaS-MT has a compacted lattice that differs in lattice twist from that of the also compacted GDP-MT. These results and the observation that EB3 promotes rapid hydrolysis of GMPCPP suggest that EB proteins modulate structural transitions at growing MT ends by recognizing and promoting an intermediate state generated during GTP hydrolysis. Our findings explain both EBs end-tracking behavior and their effect on microtubule dynamics.
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Mechanistic Origin of Microtubule Dynamic Instability and Its Modulation by EB Proteins.,Zhang R, Alushin GM, Brown A, Nogales E Cell. 2015 Jul 28. pii: S0092-8674(15)00849-1. doi: 10.1016/j.cell.2015.07.012. PMID:26234155<ref>PMID:26234155</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 3jaw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Nogales, E]]
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[[Category: Nogales E]]
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[[Category: Zhang, R]]
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[[Category: Zhang R]]
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[[Category: Eb3]]
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[[Category: Microtubule]]
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[[Category: Seam]]
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[[Category: Structural protein]]
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Current revision

Atomic model of a microtubule seam based on a cryo-EM reconstruction of the EB3-bound microtubule (merged dataset containing tubulin bound to GTPgammaS, GMPCPP, and GDP)

3jaw, resolution 3.90Å

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OCA

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