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==Crystal structure of tubulin-RB3-TTL-Zampanolide complex==
==Crystal structure of tubulin-RB3-TTL-Zampanolide complex==
<StructureSection load='4i4t' size='340' side='right' caption='[[4i4t]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='4i4t' size='340' side='right'caption='[[4i4t]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4i4t]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I4T FirstGlance]. <br>
<table><tr><td colspan='2'>[[4i4t]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I4T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TYR:TYROSINE'>TYR</scene>, <scene name='pdbligand=ZPN:(2Z,4E)-N-[(S)-[(1S,2E,5S,8E,10Z,17S)-3,11-DIMETHYL-19-METHYLIDENE-7,13-DIOXO-6,21-DIOXABICYCLO[15.3.1]HENICOSA-2,8,10-TRIEN-5-YL](HYDROXY)METHYL]HEXA-2,4-DIENAMIDE'>ZPN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TYR:TYROSINE'>TYR</scene>, <scene name='pdbligand=ZPN:(2Z,4E)-N-[(S)-[(1S,2E,5S,8E,10Z,17S)-3,11-DIMETHYL-19-METHYLIDENE-7,13-DIOXO-6,21-DIOXABICYCLO[15.3.1]HENICOSA-2,8,10-TRIEN-5-YL](HYDROXY)METHYL]HEXA-2,4-DIENAMIDE'>ZPN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i50|4i50]], [[4i55|4i55]], [[4ihj|4ihj]], [[4iij|4iij]]</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=4i4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i4t OCA], [https://pdbe.org/4i4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i4t RCSB], [https://www.ebi.ac.uk/pdbsum/4i4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i4t ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Stmn4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), TTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i4t OCA], [http://pdbe.org/4i4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i4t RCSB], [http://www.ebi.ac.uk/pdbsum/4i4t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i4t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TBA1B_BOVIN TBA1B_BOVIN]] 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/STMN4_RAT STMN4_RAT]] Exhibits microtubule-destabilizing activity.<ref>PMID:15039434</ref> <ref>PMID:12111843</ref> <ref>PMID:15014504</ref>  [[http://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] 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 (By similarity).  
[https://www.uniprot.org/uniprot/TBA1B_BOVIN TBA1B_BOVIN] 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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4i4t" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4i4t" style="background-color:#fffaf0;"></div>
==See Also==
*[[Stathmin-4 3D structures|Stathmin-4 3D structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
*[[Tubulin tyrosine ligase|Tubulin tyrosine ligase]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Buffalo rat]]
[[Category: Gallus gallus]]
[[Category: Chick]]
[[Category: Large Structures]]
[[Category: Prota, A E]]
[[Category: Rattus norvegicus]]
[[Category: Steinmetz, M O]]
[[Category: Prota AE]]
[[Category: Alpha-tubulin]]
[[Category: Steinmetz MO]]
[[Category: Beta-tubulin]]
[[Category: Cell cycle]]
[[Category: Gtpase]]
[[Category: Ligase]]
[[Category: Stathmin]]
[[Category: Zamanolide]]

Revision as of 11:41, 9 November 2022

Crystal structure of tubulin-RB3-TTL-Zampanolide complexCrystal structure of tubulin-RB3-TTL-Zampanolide complex

Structural highlights

4i4t is a 6 chain structure with sequence from Bos taurus, Gallus gallus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TBA1B_BOVIN 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.

Publication Abstract from PubMed

Microtubule-stabilizing agents (MSAs) are efficacious chemotherapeutic drugs widely used for the treatment of cancer. Despite the importance of MSAs for medical applications and basic research, their molecular mechanisms of action on tubulin and microtubules remain elusive. Here, we determined high-resolution crystal structures of alphabeta-tubulin in complex with two unrelated MSAs, zampanolide and epothilone A. Both compounds were bound to the taxane-pocket of beta-tubulin and used their respective side chain to induce structuring of the M-loop into a short helix. Because the M-loop establishes lateral tubulin contacts in microtubules, these findings explain how taxane-site MSAs promote microtubule assembly and stability. They further offer fundamental structural insights into the control mechanisms of microtubule dynamics.

Molecular Mechanism of Action of Microtubule-Stabilizing Anticancer Agents.,Prota AE, Bargsten K, Zurwerra D, Field JJ, Diaz JF, Altmann KH, Steinmetz MO Science. 2013 Jan 3. PMID:23287720[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Prota AE, Bargsten K, Zurwerra D, Field JJ, Diaz JF, Altmann KH, Steinmetz MO. Molecular Mechanism of Action of Microtubule-Stabilizing Anticancer Agents. Science. 2013 Jan 3. PMID:23287720 doi:http://dx.doi.org/10.1126/science.1230582

4i4t, resolution 1.80Å

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