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==Ustilago maydis kinesin-5 motor domain with N-terminal extension in the AMPPNP state bound to microtubules==
==Ustilago maydis kinesin-5 motor domain with N-terminal extension in the AMPPNP state bound to microtubules==
<StructureSection load='5mm7' size='340' side='right' caption='[[5mm7]], [[Resolution|resolution]] 5.10&Aring;' scene=''>
<SX load='5mm7' size='340' side='right' viewer='molstar' caption='[[5mm7]], [[Resolution|resolution]] 5.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5mm7]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MM7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MM7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5mm7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] and [https://en.wikipedia.org/wiki/Ustilago_maydis Ustilago maydis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MM7 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.1&#8491;</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=5mm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mm7 OCA], [http://pdbe.org/5mm7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mm7 RCSB], [http://www.ebi.ac.uk/pdbsum/5mm7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mm7 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></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=5mm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mm7 OCA], [https://pdbe.org/5mm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mm7 RCSB], [https://www.ebi.ac.uk/pdbsum/5mm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mm7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TBB_PIG TBB_PIG]] 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/TBA1A_PIG TBA1A_PIG]] 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.
[https://www.uniprot.org/uniprot/A0A0D1DQH0_MYCMD A0A0D1DQH0_MYCMD]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In many eukaryotes, kinesin-5 motors are essential for mitosis, and small molecules that inhibit human kinesin-5 disrupt cell division. To investigate whether fungal kinesin-5s could be targets for novel fungicides, we studied kinesin-5 from the pathogenic fungus Ustilago maydis. We used cryo-electron microscopy to determine the microtubule-bound structure of its motor domain with and without the N-terminal extension. The ATP-like conformations of the motor in the presence or absence of this N-terminus are very similar, suggesting this region is structurally disordered and does not directly influence the motor ATPase. The Ustilago maydis kinesin-5 motor domain adopts a canonical ATP-like conformation, thereby allowing the neck linker to bind along the motor domain towards the microtubule plus end. However, several insertions within this motor domain are structurally distinct. Loop2 forms a non-canonical interaction with alpha-tubulin, while loop8 may bridge between two adjacent protofilaments. Furthermore, loop5 - which in human kinesin-5 is involved in binding allosteric inhibitors - protrudes above the nucleotide binding site, revealing a distinct binding pocket for potential inhibitors. This work highlights fungal-specific elaborations of the kinesin-5 motor domain and provides the structural basis for future investigations of kinesins as targets for novel fungicides.
 
Cryo-EM structure of the Ustilago maydis kinesin-5 motor domain bound to microtubules.,von Loeffelholz O, Moores CA J Struct Biol. 2019 Jul 6. pii: S1047-8477(19)30139-X. doi:, 10.1016/j.jsb.2019.07.003. PMID:31288039<ref>PMID:31288039</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mm7" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Kinesin 3D Structures|Kinesin 3D Structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Loeffelholz, O von]]
[[Category: Large Structures]]
[[Category: Moores, C A]]
[[Category: Sus scrofa]]
[[Category: Kinesin-5]]
[[Category: Ustilago maydis]]
[[Category: Motor protein]]
[[Category: Moores CA]]
[[Category: Ustilago maydi]]
[[Category: Von Loeffelholz O]]