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| | <StructureSection load='4u3j' size='340' side='right'caption='[[4u3j]], [[Resolution|resolution]] 2.81Å' scene=''> | | <StructureSection load='4u3j' size='340' side='right'caption='[[4u3j]], [[Resolution|resolution]] 2.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4u3j]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U3J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4u3j]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U3J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.81Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TUB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), TUB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), STU2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u3j OCA], [http://pdbe.org/4u3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u3j RCSB], [http://www.ebi.ac.uk/pdbsum/4u3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u3j 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=4u3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u3j OCA], [https://pdbe.org/4u3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u3j RCSB], [https://www.ebi.ac.uk/pdbsum/4u3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u3j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. [[http://www.uniprot.org/uniprot/STU2_YEAST STU2_YEAST]] May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body. [[http://www.uniprot.org/uniprot/TBB_YEAST TBB_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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Tubulin|Tubulin]] | + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ayaz, P]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Rice, L M]] | + | [[Category: Ayaz P]] |
| - | [[Category: Complex]] | + | [[Category: Rice LM]] |
| - | [[Category: Structural protein-protein binding complex]]
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| Structural highlights
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.
Publication Abstract from PubMed
Stu2p/XMAP215 proteins are essential microtubule polymerases that use multiple alphabeta-tubulin-interacting TOG domains to bind microtubule plus ends and catalyze fast microtubule growth. We report here the structure of the TOG2 domain from Stu2p bound to yeast alphabeta-tubulin. Like TOG1, TOG2 binds selectively to a fully 'curved' conformation of alphabeta-tubulin, incompatible with a microtubule lattice. We also show that TOG1-TOG2 binds non-cooperatively to two alphabeta-tubulins. Preferential interactions between TOGs and fully curved alphabeta-tubulin that cannot exist elsewhere in the microtubule explain how these polymerases localize to the extreme microtubule end. We propose that these polymerases promote elongation because their linked TOG domains concentrate unpolymerized alphabeta-tubulin near curved subunits already bound at the microtubule end. This tethering model can explain catalyst-like behavior and also predicts that the polymerase action changes the configuration of the microtubule end.
A tethered delivery mechanism explains the catalytic action of a microtubule polymerase.,Ayaz P, Munyoki S, Geyer EA, Piedra FA, Vu ES, Bromberg R, Otwinowski Z, Grishin NV, Brautigam CA, Rice LM Elife. 2014 Aug 5:e03069. doi: 10.7554/eLife.03069. PMID:25097237[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ayaz P, Munyoki S, Geyer EA, Piedra FA, Vu ES, Bromberg R, Otwinowski Z, Grishin NV, Brautigam CA, Rice LM. A tethered delivery mechanism explains the catalytic action of a microtubule polymerase. Elife. 2014 Aug 5:e03069. doi: 10.7554/eLife.03069. PMID:25097237 doi:http://dx.doi.org/10.7554/eLife.03069
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