4ffb: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ffb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FFB FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ffb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FFB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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">X-ray diffraction, [[Resolution|Resolution]] 2.882&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4ffb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffb OCA], [https://pdbe.org/4ffb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ffb RCSB], [https://www.ebi.ac.uk/pdbsum/4ffb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ffb 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=4ffb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffb OCA], [https://pdbe.org/4ffb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ffb RCSB], [https://www.ebi.ac.uk/pdbsum/4ffb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ffb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/TBA1_YEAST TBA1_YEAST] 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/TBA1_YEAST TBA1_YEAST] 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 ==
Stu2p/XMAP215/Dis1 family proteins are evolutionarily conserved regulatory factors that use alphabeta-tubulin-interacting tumor overexpressed gene (TOG) domains to catalyze fast microtubule growth. Catalysis requires that these polymerases discriminate between unpolymerized and polymerized forms of alphabeta-tubulin, but the mechanism by which they do so has remained unclear. Here, we report the structure of the TOG1 domain from Stu2p bound to yeast alphabeta-tubulin. TOG1 binds alphabeta-tubulin in a way that excludes equivalent binding of a second TOG domain. Furthermore, TOG1 preferentially binds a curved conformation of alphabeta-tubulin that cannot be incorporated into microtubules, contacting alpha- and beta-tubulin surfaces that do not participate in microtubule assembly. Conformation-selective interactions with alphabeta-tubulin explain how TOG-containing polymerases discriminate between unpolymerized and polymerized forms of alphabeta-tubulin and how they selectively recognize the growing end of the microtubule.
A TOG:alphabeta-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase.,Ayaz P, Ye X, Huddleston P, Brautigam CA, Rice LM Science. 2012 Aug 17;337(6096):857-60. PMID:22904013<ref>PMID:22904013</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ffb" 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__
</StructureSection>
</StructureSection>

Latest revision as of 18:23, 14 March 2024

A TOG:alpha/beta-tubulin Complex Structure Reveals Conformation-Based Mechanisms For a Microtubule PolymeraseA TOG:alpha/beta-tubulin Complex Structure Reveals Conformation-Based Mechanisms For a Microtubule Polymerase

Structural highlights

4ffb is a 3 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.882Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TBA1_YEAST 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.

See Also

4ffb, resolution 2.88Å

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