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| | <StructureSection load='3hkb' size='340' side='right'caption='[[3hkb]], [[Resolution|resolution]] 3.65Å' scene=''> | | <StructureSection load='3hkb' size='340' side='right'caption='[[3hkb]], [[Resolution|resolution]] 3.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hkb]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HKB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hkb]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries] 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=3HKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HKB 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">X-ray diffraction, [[Resolution|Resolution]] 3.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sa0|1sa0]], [[1sa1|1sa1]], [[3hkc|3hkc]], [[3hkd|3hkd]], [[3hke|3hke]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Stmn4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3hkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hkb OCA], [https://pdbe.org/3hkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hkb RCSB], [https://www.ebi.ac.uk/pdbsum/3hkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hkb 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=3hkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hkb OCA], [https://pdbe.org/3hkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hkb RCSB], [https://www.ebi.ac.uk/pdbsum/3hkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hkb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/STMN4_RAT STMN4_RAT]] Exhibits microtubule-destabilizing activity.<ref>PMID:15039434</ref> <ref>PMID:12111843</ref> <ref>PMID:15014504</ref>
| + | [https://www.uniprot.org/uniprot/D0VWZ0_SHEEP D0VWZ0_SHEEP] 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).[RuleBase:RU003505][SAAS:SAAS023123_004_019801] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Ovis aries]] | | [[Category: Ovis aries]] |
| - | [[Category: Dorleans, A]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Gigant, B]] | + | [[Category: Dorleans A]] |
| - | [[Category: Knossow, M]] | + | [[Category: Gigant B]] |
| - | [[Category: Mailliet, P]] | + | [[Category: Knossow M]] |
| - | [[Category: Mikol, V]] | + | [[Category: Mailliet P]] |
| - | [[Category: Ravelli, R B.G]] | + | [[Category: Mikol V]] |
| - | [[Category: Alpha-tubulin]]
| + | [[Category: Ravelli RBG]] |
| - | [[Category: Beta-tubulin]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Microtubule]]
| + | |
| - | [[Category: Stathmin]]
| + | |
| - | [[Category: Tubulin]]
| + | |
| Structural highlights
Function
D0VWZ0_SHEEP 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).[RuleBase:RU003505][SAAS:SAAS023123_004_019801]
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
Structural changes occur in the alphabeta-tubulin heterodimer during the microtubule assembly/disassembly cycle. Their most prominent feature is a transition from a straight, microtubular structure to a curved structure. There is a broad range of small molecule compounds that disturbs the microtubule cycle, a class of which targets the colchicine-binding site and prevents microtubule assembly. This class includes compounds with very different chemical structures, and it is presently unknown whether they prevent tubulin polymerization by the same mechanism. To address this issue, we have determined the structures of tubulin complexed with a set of such ligands and show that they interfere with several of the movements of tubulin subunits structural elements upon its transition from curved to straight. We also determined the structure of tubulin unliganded at the colchicine site; this reveals that a beta-tubulin loop (termed T7) flips into this site. As with colchicine site ligands, this prevents a helix which is at the interface with alpha-tubulin from stacking onto a beta-tubulin beta sheet as in straight protofilaments. Whereas in the presence of these ligands the interference with microtubule assembly gets frozen, by flipping in and out the beta-subunit T7 loop participates in a reversible way in the resistance to straightening that opposes microtubule assembly. Our results suggest that it thereby contributes to microtubule dynamic instability.
Variations in the colchicine-binding domain provide insight into the structural switch of tubulin.,Dorleans A, Gigant B, Ravelli RB, Mailliet P, Mikol V, Knossow M Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13775-9. Epub 2009 Aug 5. PMID:19666559[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dorleans A, Gigant B, Ravelli RB, Mailliet P, Mikol V, Knossow M. Variations in the colchicine-binding domain provide insight into the structural switch of tubulin. Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13775-9. Epub 2009 Aug 5. PMID:19666559
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