View source for 7pqc


==tau-microtubule structural ensemble based on CryoEM data==
<StructureSection load='7pqc' size='340' side='right'caption='[[7pqc]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pqc]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=7PQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PQC 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]] 4.1&#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></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=7pqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pqc OCA], [https://pdbe.org/7pqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pqc RCSB], [https://www.ebi.ac.uk/pdbsum/7pqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pqc ProSAT]</span></td></tr>
</table>
== Function ==
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tau is a microtubule-associated protein that regulates the stability of microtubules. We use metainference cryoelectron microscopy, an integrative structural biology approach, to determine an ensemble of conformations representing the structure and dynamics of a tau-microtubule complex comprising the entire microtubule-binding region of tau (residues 202-395). We thus identify the ground state of the complex and a series of excited states of lower populations. A comparison of the interactions in these different states reveals positions along the tau sequence that are important to determine the overall stability of the tau-microtubule complex. This analysis leads to the identification of positions where phosphorylation and acetylation events have destabilizing effects, which we validate by using site-specific post-translationally modified tau variants obtained by chemical mutagenesis. Taken together, these results illustrate how the simultaneous determination of ground and excited states of macromolecular complexes reveals functional and regulatory mechanisms.

A Structural Ensemble of a Tau-Microtubule Complex Reveals Regulatory Tau Phosphorylation and Acetylation Mechanisms.,Brotzakis ZF, Lindstedt PR, Taylor RJ, Rinauro DJ, Gallagher NCT, Bernardes GJL, Vendruscolo M ACS Cent Sci. 2021 Dec 22;7(12):1986-1995. doi: 10.1021/acscentsci.1c00585. Epub , 2021 Dec 8. PMID:34963892<ref>PMID:34963892</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pqc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
*[[Tau protein 3D structures|Tau protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Brotzakis ZF]]
[[Category: Vendruscolo M]]