3t0q

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<StructureSection load='3t0q' size='340' side='right'caption='[[3t0q]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='3t0q' size='340' side='right'caption='[[3t0q]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t0q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ashgo Ashgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t0q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eremothecium_gossypii_ATCC_10895 Eremothecium gossypii ATCC 10895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0Q FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AGOS_AGR253W, AGR253W, AGR253Wp ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284811 ASHGO])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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'>[https://proteopedia.org/fgij/fg.htm?mol=3t0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0q OCA], [https://pdbe.org/3t0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0q RCSB], [https://www.ebi.ac.uk/pdbsum/3t0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0q ProSAT]</span></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=3t0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0q OCA], [https://pdbe.org/3t0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0q RCSB], [https://www.ebi.ac.uk/pdbsum/3t0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0q ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q74ZE6_ASHGO Q74ZE6_ASHGO]
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Kar3 kinesins are microtubule (MT) minus-end-directed motors with pleiotropic functions in mitotic spindle formation and nuclear movement in budding and fission yeasts. A Kar3-like kinesin is also expressed by the filamentous fungus Ashbya gossypi, which exhibits different nuclear movement challenges from its yeast relatives. Presented here is a 2.35 A crystal structure and enzymatic analysis of the AgKar3 motor domain (AgKar3MD). Compared to the previously published Saccharomyces cerevisiae Kar3MD structure (ScKar3MD), AgKar3MD displays differences in the conformation of some of its nucleotide-binding motifs and peripheral elements. Unlike ScKar3MD, the salt bridge between Switch I and Switch II in AgKar3MD is broken. Most of the Switch I, and the adjoining region of helix alpha3, are also disordered instead of bending into the active site cleft as is observed in ScKar3MD. These aspects of AgKar3MD are highly reminiscent of the ScKar3 R598A mutant that disrupts the Switch I-Switch II salt bridge and impairs MT-stimulated ATPase activity of the motor. Subtle differences in the disposition of secondary structure elements in the small lobe (beta1a, beta1b, and beta1c) at the edge of the MD are also apparent even though it contains approximately the same number of residues as ScKar3. These differences may reflect the unique enzymatic properties we measured for this motor, which include a lower MT-stimulated ATPase rate relative to ScKar3, or they could relate to its interactions with different regulatory companion proteins than its budding yeast counterpart.
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Crystal structure of the Kar3-like kinesin motor domain from the filamentous fungus Ashbya gossypii.,Duan D, Hnatchuk DJ, Brenner J, Davis D, Allingham JS Proteins. 2012 Apr;80(4):1016-27. PMID:22493778<ref>PMID:22493778</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3t0q" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ashgo]]
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[[Category: Eremothecium gossypii ATCC 10895]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Allingham, J S]]
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[[Category: Allingham JS]]
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[[Category: Brenner, J]]
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[[Category: Brenner J]]
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[[Category: Davis, D]]
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[[Category: Davis D]]
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[[Category: Duan, D]]
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[[Category: Duan D]]
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[[Category: Hnatchuk, D J]]
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[[Category: Hnatchuk DJ]]
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[[Category: Alpha and beta protein]]
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[[Category: Atp binding]]
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[[Category: Kinesin]]
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[[Category: Microtubule motor protein]]
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[[Category: Motor protein]]
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[[Category: P-loop containing nucleoside triphosphate hydrolase]]
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Current revision

Motor Domain Structure of the Kar3-like kinesin from Ashbya gossypii

PDB ID 3t0q

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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