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3pxn

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Crystal structure of the Drosophila kinesin family member Kin10/NOD in complex with divalent manganese and ADP

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 <StructureSection load='3pxn' size='340' side='right'caption='[[3pxn]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3pxn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3pxn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXN FirstGlance]. <br>
-</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=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dc4|3dc4]], [[3dcb|3dcb]], [[3dco|3dco]]</div></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=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nod, NODA, CG1763 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=3pxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxn OCA], [https://pdbe.org/3pxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxn RCSB], [https://www.ebi.ac.uk/pdbsum/3pxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/NOD_DROME NOD_DROME]] Required for the distributive chromosome segregation of non-exchange chromosomes during meiosis. May be a microtubule motor required to hold distributively "paired" chromosomes at the metaphase plate until anaphase.
+[https://www.uniprot.org/uniprot/NOD_DROME NOD_DROME] Required for the distributive chromosome segregation of non-exchange chromosomes during meiosis. May be a microtubule motor required to hold distributively "paired" chromosomes at the metaphase plate until anaphase.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Kinesins are molecular motors that require a divalent metal ion (for example, Mg(2+)) to convert the energy of ATP hydrolysis into directed force production along microtubules. Here we present the crystal structure of a recombinant kinesin motor domain bound to Mn(2+) and ADP and report on a serine-to-cysteine substitution in the switch 1 motif of kinesin that allows its ATP hydrolysis activity to be controlled by adjusting the ratio of Mn(2+) to Mg(2+). This mutant kinesin binds ATP similarly in the presence of either metal ion, but its ATP hydrolysis activity is greatly diminished in the presence of Mg(2+). In human kinesin-1 and kinesin-5 as well as Drosophila melanogaster kinesin-10 and kinesin-14, this defect is rescued by Mn(2+), providing a way to control both the enzymatic activity and force-generating ability of these nanomachines.
-A metal switch for controlling the activity of molecular motor proteins.,Cochran JC, Zhao YC, Wilcox DE, Kull FJ Nat Struct Mol Biol. 2011 Dec 25;19(1):122-7. doi: 10.1038/nsmb.2190. PMID:22198464<ref>PMID:22198464</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3pxn" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
 [[Category: Large Structures]]
-[[Category: Cochran, J C]]
+[[Category: Cochran JC]]
-[[Category: Kull, F J]]
+[[Category: Kull FJ]]
-[[Category: Wilcox, D E]]
+[[Category: Wilcox DE]]
-[[Category: Zhao, Y C]]
+[[Category: Zhao YC]]
-[[Category: Alpha/beta class]]
-[[Category: Atp hydrolysis]]
-[[Category: Atp-binding]]
-[[Category: Cell cycle]]
-[[Category: Cell division]]
-[[Category: Kinesin]]
-[[Category: Meiosis]]
-[[Category: Microtubule]]
-[[Category: Motor domain]]
-[[Category: Motor protein]]
-[[Category: Nucleotide-binding]]
-[[Category: Spindle protein]]

3pxn

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Crystal structure of the Drosophila kinesin family member Kin10/NOD in complex with divalent manganese and ADP

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