3hkd: Difference between revisions
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==Tubulin-TN16 : RB3 stathmin-like domain complex== | ==Tubulin-TN16 : RB3 stathmin-like domain complex== | ||
<StructureSection load='3hkd' size='340' side='right' caption='[[3hkd]], [[Resolution|resolution]] 3.70Å' scene=''> | <StructureSection load='3hkd' size='340' side='right'caption='[[3hkd]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3hkd]] is a 5 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3hkd]] 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=3HKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HKD 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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=N16:(3Z,5S)-5-BENZYL-3-[1-(PHENYLAMINO)ETHYLIDENE]PYRROLIDINE-2,4-DIONE'>N16</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7Å</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>, <scene name='pdbligand=N16:(3Z,5S)-5-BENZYL-3-[1-(PHENYLAMINO)ETHYLIDENE]PYRROLIDINE-2,4-DIONE'>N16</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=3hkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hkd OCA], [https://pdbe.org/3hkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hkd RCSB], [https://www.ebi.ac.uk/pdbsum/3hkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hkd ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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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==See Also== | ==See Also== | ||
*[[Stathmin|Stathmin]] | *[[Stathmin-4 3D structures|Stathmin-4 3D structures]] | ||
*[[Tubulin|Tubulin | *[[Tubulin 3D Structures|Tubulin 3D Structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ovis aries]] | [[Category: Ovis aries]] | ||
[[Category: Dorleans | [[Category: Rattus norvegicus]] | ||
[[Category: Gigant | [[Category: Dorleans A]] | ||
[[Category: Knossow | [[Category: Gigant B]] | ||
[[Category: Mailliet | [[Category: Knossow M]] | ||
[[Category: Mikol | [[Category: Mailliet P]] | ||
[[Category: Ravelli | [[Category: Mikol V]] | ||
[[Category: Ravelli RBG]] | |||
Latest revision as of 18:50, 1 November 2023
Tubulin-TN16 : RB3 stathmin-like domain complexTubulin-TN16 : RB3 stathmin-like domain complex
Structural highlights
FunctionD0VWZ0_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 PubMedStructural 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 AlsoReferences |
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