View source for 9hq4


==TTLL11 bound to microtubule==
<StructureSection load='9hq4' size='340' side='right'caption='[[9hq4]], [[Resolution|resolution]] 3.28&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9hq4]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Pseudomonas_pavonaceae Pseudomonas pavonaceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HQ4 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]] 3.28&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</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=9hq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hq4 OCA], [https://pdbe.org/9hq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hq4 RCSB], [https://www.ebi.ac.uk/pdbsum/9hq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hq4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TBA1B_HUMAN TBA1B_HUMAN] 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 ==
Microtubules (MTs) undergo diverse posttranslational modifications that regulate their structural and functional properties. Among these, polyglutamylation-a dominant and conserved modification targeting unstructured tubulin C-terminal tails-plays a pivotal role in defining the tubulin code. Here, we describe a mechanism by which tubulin tyrosine ligase-like 11 (TTLL11) expands and diversifies the code. Cryo-electron microscopy revealed a unique bipartite MT recognition strategy wherein TTLL11 binding and catalytic domains engage adjacent MT protofilaments. Biochemical and cellular assays identified previously uncharacterized polyglutamylation patterns, showing that TTLL11 directly extends the primary polypeptide chains of alpha- and beta-tubulin in vitro, challenging the prevailing paradigms emphasizing lateral branching. Moreover, cell-based and in vivo data suggest a cross-talk between polyglutamylation and the detyrosination/tyrosination cycle likely linked to the TTLL11-mediated elongation of the primary alpha-tubulin chain. These findings unveil an unrecognized layer of complexity within the tubulin code and offer mechanistic insights into the molecular basis of functional specialization of MT cytoskeleton.

Mechanistic insights into TTLL11 polyglutamylase-mediated primary tubulin chain elongation.,Campbell J, Vosahlikova M, Ismail S, Volnikova M, Motlova L, Kudlacova J, Ustinova K, Snajdr I, Novakova Z, Basta M, Gutsche I, Moutin MJ, Desfosses A, Barinka C Sci Adv. 2025 Aug 22;11(34):eadw1561. doi: 10.1126/sciadv.adw1561. Epub 2025 Aug , 20. PMID:40834096<ref>PMID:40834096</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 9hq4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Pseudomonas pavonaceae]]
[[Category: Barinka C]]
[[Category: Campbell J]]
[[Category: Desfosses A]]
[[Category: Gutsche I]]