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| <StructureSection load='1ffx' size='340' side='right'caption='[[1ffx]], [[Resolution|resolution]] 3.95Å' scene=''> | | <StructureSection load='1ffx' size='340' side='right'caption='[[1ffx]], [[Resolution|resolution]] 3.95Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1ffx]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. The July 2014 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Microtubules'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2014_7 10.2210/rcsb_pdb/mom_2014_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FFX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ffx]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. The July 2014 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Microtubules'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2014_7 10.2210/rcsb_pdb/mom_2014_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FFX FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</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]] 3.95Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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></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=1ffx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffx OCA], [http://pdbe.org/1ffx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ffx RCSB], [http://www.ebi.ac.uk/pdbsum/1ffx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffx 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=1ffx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffx OCA], [https://pdbe.org/1ffx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ffx RCSB], [https://www.ebi.ac.uk/pdbsum/1ffx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffx ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/TBA1A_PIG TBA1A_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/TBA1A_PIG TBA1A_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. |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | | |
| ==See Also== | | ==See Also== |
- | *[[Tubulin|Tubulin]] | + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
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| </StructureSection> | | </StructureSection> |
| [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
- | [[Category: Buffalo rat]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Microtubules]] | | [[Category: Microtubules]] |
| [[Category: RCSB PDB Molecule of the Month]] | | [[Category: RCSB PDB Molecule of the Month]] |
- | [[Category: Gigant, B]] | + | [[Category: Rattus norvegicus]] |
- | [[Category: Knossow, M]] | + | [[Category: Gigant B]] |
- | [[Category: Martin-Barbey, C]] | + | [[Category: Knossow M]] |
- | [[Category: Alpha-tubulin]]
| + | [[Category: Martin-Barbey C]] |
- | [[Category: Beta-tubulin]]
| + | |
- | [[Category: Microtubule]]
| + | |
- | [[Category: Stathmin]]
| + | |
- | [[Category: Structural protein]]
| + | |
- | [[Category: Tubulin]]
| + | |
| Structural highlights
Function
TBA1A_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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Phosphoproteins of the stathmin family interact with the alphabeta tubulin heterodimer (tubulin) and hence interfere with microtubule dynamics. The structure of the complex of GDP-tubulin with the stathmin-like domain of the neural protein RB3 reveals a head-to-tail assembly of two tubulins with a 91-residue RB3 alpha helix in which each copy of an internal duplicated sequence interacts with a different tubulin. As a result of the relative orientations adopted by tubulins and by their alpha and beta subunits, the tubulin:RB3 complex forms a curved structure. The RB3 helix thus most likely prevents incorporation of tubulin into microtubules by holding it in an assembly with a curvature very similar to that of the depolymerization products of microtubules.
The 4 A X-ray structure of a tubulin:stathmin-like domain complex.,Gigant B, Curmi PA, Martin-Barbey C, Charbaut E, Lachkar S, Lebeau L, Siavoshian S, Sobel A, Knossow M Cell. 2000 Sep 15;102(6):809-16. PMID:11030624[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gigant B, Curmi PA, Martin-Barbey C, Charbaut E, Lachkar S, Lebeau L, Siavoshian S, Sobel A, Knossow M. The 4 A X-ray structure of a tubulin:stathmin-like domain complex. Cell. 2000 Sep 15;102(6):809-16. PMID:11030624
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