4uy0
From Proteopedia
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| - | ''' | + | ==Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins== |
| + | <StructureSection load='4uy0' size='340' side='right' caption='[[4uy0]], [[Resolution|resolution]] 7.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4uy0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UY0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UY0 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uxo|4uxo]], [[4uxp|4uxp]], [[4uxr|4uxr]], [[4uxs|4uxs]], [[4uxt|4uxt]], [[4uxy|4uxy]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uy0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uy0 RCSB], [http://www.ebi.ac.uk/pdbsum/4uy0 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/KIF5A_HUMAN KIF5A_HUMAN]] Autosomal dominant spastic paraplegia type 10;Autosomal dominant Charcot-Marie-Tooth disease type 2 due to KIF5A mutation. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:12355402</ref> <ref>PMID:15452312</ref> <ref>PMID:16476820</ref> <ref>PMID:16489470</ref> <ref>PMID:18203753</ref> <ref>PMID:18245137</ref> <ref>PMID:18853458</ref> <ref>PMID:21107874</ref> | ||
| + | == 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/KIF5A_HUMAN KIF5A_HUMAN]] Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL) (By similarity). [[http://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_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 (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Kinesins are a superfamily of microtubule-based ATP-powered motors, important for multiple, essential cellular functions. How microtubule binding stimulates their ATPase and controls force generation is not understood. To address this fundamental question, we visualized microtubule-bound kinesin-1 and kinesin-3 motor domains at multiple steps in their ATPase cycles - including their nucleotide-free states - at ~7A resolution using cryo-electron microscopy. In both motors, microtubule binding promotes ordered conformations of conserved loops that stimulate ADP release, enhance microtubule affinity and prime the catalytic site for ATP binding. ATP binding causes only small shifts of these nucleotide-coordinating loops but induces large conformational changes elsewhere that allow force generation and neck linker docking towards the microtubule plus end. Family-specific differences across the kinesin-microtubule interface account for the distinctive properties of each motor. Our data thus provide evidence for a conserved ATP-driven mechanism for kinesins and reveal the critical mechanistic contribution of the microtubule interface. | ||
| - | + | Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins.,Atherton J, Farabella I, Yu IM, Rosenfeld SS, Houdusse A, Topf M, Moores CA Elife. 2014 Sep 10:e03680. doi: 10.7554/eLife.03680. PMID:25209998<ref>PMID:25209998</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Atherton, J.]] | ||
| + | [[Category: Farabella, I.]] | ||
| + | [[Category: Houdusse, A.]] | ||
| + | [[Category: Moores, C.]] | ||
| + | [[Category: Rosenfeld, S S.]] | ||
| + | [[Category: Topf, M.]] | ||
| + | [[Category: Yu, I M.]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 10:21, 24 September 2014
Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
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