5mio
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==KIF2C-DARPIN FUSION PROTEIN BOUND TO TUBULIN== | |
| + | <StructureSection load='5mio' size='340' side='right' caption='[[5mio]], [[Resolution|resolution]] 3.19Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mio]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ ], [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MIO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MIO FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=LOC:N-[(7S)-1,2,3,10-TETRAMETHOXY-9-OXO-6,7-DIHYDRO-5H-BENZO[D]HEPTALEN-7-YL]ETHANAMIDE'>LOC</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=5mio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mio OCA], [http://pdbe.org/5mio PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mio RCSB], [http://www.ebi.ac.uk/pdbsum/5mio PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mio ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TBA1B_BOVIN TBA1B_BOVIN]] 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/KIF2C_HUMAN KIF2C_HUMAN]] In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis.<ref>PMID:19060894</ref> <ref>PMID:21820309</ref> [[http://www.uniprot.org/uniprot/D0VWY9_SHEEP 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] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Kinesin-13s are critical microtubule regulators which induce microtubule disassembly in an ATP dependent manner. To clarify their mechanism, we report here the crystal structure of a functional construct of the kinesin-13 Kif2C/MCAK in an ATP-like state and bound to the alphabeta-tubulin heterodimer, a complex mimicking the species that dissociates from microtubule ends during catalytic disassembly. Our results picture how Kif2C stabilizes a curved tubulin conformation. The Kif2C alpha4-L12-alpha5 region undergoes a remarkable 25 degrees rotation upon tubulin binding to target the alphabeta-tubulin hinge. This movement leads the beta5a-beta5b motif to interact with the distal end of beta-tubulin, whereas the neck and the KVD motif, two specific elements of kinesin-13s, target the alpha-tubulin distal end. Taken together with the study of Kif2C mutants, our data suggest that stabilization of a curved tubulin is an important contribution to the Kif2C mechanism.Kinesin-13s are microtubule depolymerizing enzymes. Here the authors present the crystal structure of a DARPin fused construct comprising the short neck region and motor domain of kinesin-13 in complex with an alphabeta-tubulin heterodimer, which shows that kinesin-13 functions by stabilizing a curved tubulin conformation. | ||
| - | + | Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin.,Wang W, Cantos-Fernandes S, Lv Y, Kuerban H, Ahmad S, Wang C, Gigant B Nat Commun. 2017 Jul 10;8(1):70. doi: 10.1038/s41467-017-00091-9. PMID:28694425<ref>PMID:28694425</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5mio" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Ovis aries]] | ||
| + | [[Category: GIGANT, B]] | ||
| + | [[Category: WANG, W]] | ||
| + | [[Category: Kinesin-13 microtubule atpase motor protein]] | ||
| + | [[Category: Motor protein]] | ||
Revision as of 03:52, 6 September 2017
KIF2C-DARPIN FUSION PROTEIN BOUND TO TUBULIN
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