4f61: Difference between revisions
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==Tubulin:Stathmin-like domain complex== | ==Tubulin:Stathmin-like domain complex== | ||
<StructureSection load='4f61' size='340' side='right' caption='[[4f61]], [[Resolution|resolution]] 4.17Å' scene=''> | <StructureSection load='4f61' size='340' side='right' caption='[[4f61]], [[Resolution|resolution]] 4.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4f61]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] and [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4f61]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] and [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F61 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F61 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></td></tr> | </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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f6r|4f6r]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f6r|4f6r]]</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=4f61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f61 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f61 RCSB], [http://www.ebi.ac.uk/pdbsum/4f61 PDBsum]</span></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=4f61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f61 OCA], [http://pdbe.org/4f61 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f61 RCSB], [http://www.ebi.ac.uk/pdbsum/4f61 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f61 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4f61" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Ovis aries]] | [[Category: Ovis aries]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct sequences]] | ||
[[Category: Gigant, B]] | [[Category: Gigant, B]] | ||
[[Category: Knossow, M]] | [[Category: Knossow, M]] | ||
Revision as of 07:58, 5 August 2016
Tubulin:Stathmin-like domain complexTubulin:Stathmin-like domain complex
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] [D0VWY9_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] Publication Abstract from PubMedIn cells, microtubule dynamics is regulated by stabilizing and destabilizing factors. Whereas proteins in both categories have been identified, their mechanism of action is rarely understood at the molecular level. This is due in part to the difficulties faced in structural approaches to obtain atomic models when tubulin is involved. Here, we design and characterize new stathmin-like domain (SLD) proteins that sequester tubulins in numbers different from two, the number of tubulins bound by stathmin or by the SLD of RB3, two stathmin family members that have been extensively studied. We established rules for the design of tight tubulin-SLD assemblies and applied them to complexes containing one to four tubulin heterodimers. Biochemical and structural experiments showed that the engineered SLDs behaved as expected. The new SLDs will be tools for structural studies of microtubule regulation. The larger complexes will be useful for cryo-electron microscopy, whereas crystallography or nuclear magnetic resonance will benefit from the 1:1 tubulin-SLD assembly. Finally, our results provide new insight into SLD function, suggesting that a major effect of these phosphorylatable proteins is the programmed release of sequestered tubulin for microtubule assembly at the specific cellular locations of members of the stathmin family. Design and characterization of modular scaffolds for tubulin assembly.,Mignot I, Pecqueur L, Dorleans A, Karuppasamy M, Ravelli RB, Dreier B, Pluckthun A, Knossow M, Gigant B J Biol Chem. 2012 Sep 7;287(37):31085-94. Epub 2012 Jul 12. PMID:22791712[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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