6o2q: Difference between revisions

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<SX load='6o2q' size='340' side='right' viewer='molstar' caption='[[6o2q]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<SX load='6o2q' size='340' side='right' viewer='molstar' caption='[[6o2q]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6o2q]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O2Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6O2Q FirstGlance]. <br>
<table><tr><td colspan='2'>[[6o2q]] is a 12 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=6O2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O2Q FirstGlance]. <br>
</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>
</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6o2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o2q OCA], [http://pdbe.org/6o2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o2q RCSB], [http://www.ebi.ac.uk/pdbsum/6o2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o2q ProSAT]</span></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=6o2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o2q OCA], [https://pdbe.org/6o2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o2q RCSB], [https://www.ebi.ac.uk/pdbsum/6o2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o2q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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. [[http://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.  
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Acetylation of K40 in alpha-tubulin is the sole posttranslational modification to mark the luminal surface of microtubules. It is still controversial whether its relationship with microtubule stabilization is correlative or causative. We have obtained high-resolution cryo-electron microscopy (cryo-EM) reconstructions of pure samples of alphaTAT1-acetylated and SIRT2-deacetylated microtubules to visualize the structural consequences of this modification and reveal its potential for influencing the larger assembly properties of microtubules. We modeled the conformational ensembles of the unmodified and acetylated states by using the experimental cryo-EM density as a structural restraint in molecular dynamics simulations. We found that acetylation alters the conformational landscape of the flexible loop that contains alphaK40. Modification of alphaK40 reduces the disorder of the loop and restricts the states that it samples. We propose that the change in conformational sampling that we describe, at a location very close to the lateral contacts site, is likely to affect microtubule stability and function.
 
Effects of alpha-tubulin acetylation on microtubule structure and stability.,Eshun-Wilson L, Zhang R, Portran D, Nachury MV, Toso DB, Lohr T, Vendruscolo M, Bonomi M, Fraser JS, Nogales E Proc Natl Acad Sci U S A. 2019 May 21;116(21):10366-10371. doi:, 10.1073/pnas.1900441116. Epub 2019 May 9. PMID:31072936<ref>PMID:31072936</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6o2q" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Bonomi, M]]
[[Category: Bonomi M]]
[[Category: Eshun-Wilson, L]]
[[Category: Eshun-Wilson L]]
[[Category: Fraser, J S]]
[[Category: Fraser JS]]
[[Category: Lohr, T]]
[[Category: Lohr T]]
[[Category: Nachury, M V]]
[[Category: Nachury MV]]
[[Category: Nogales, E]]
[[Category: Nogales E]]
[[Category: Portran, D]]
[[Category: Portran D]]
[[Category: Toso, D]]
[[Category: Toso D]]
[[Category: Vendruscolo, M]]
[[Category: Vendruscolo M]]
[[Category: Zhang, R]]
[[Category: Zhang R]]
[[Category: Acetylation]]
[[Category: Cytoskeleton]]
[[Category: Microtubule]]
[[Category: Structural protein]]

Latest revision as of 12:22, 20 March 2024

Acetylated MicrotubulesAcetylated Microtubules

6o2q, resolution 3.70Å

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