7pqp: Difference between revisions
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==tau-microtubule structural ensemble based on CryoEM data== | |||
<StructureSection load='7pqp' size='340' side='right'caption='[[7pqp]], [[Resolution|resolution]] 4.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7pqp]] 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=7PQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PQP 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]] 4.1Å</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=7pqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pqp OCA], [https://pdbe.org/7pqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pqp RCSB], [https://www.ebi.ac.uk/pdbsum/7pqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pqp 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7pqp" style="background-color:#fffaf0;"></div> | ||
[[Category: Brotzakis | |||
==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]] | |||
Latest revision as of 12:33, 17 July 2024
tau-microtubule structural ensemble based on CryoEM data
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