5wc1: Difference between revisions
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==katanin AAA ATPase domain== | ==katanin AAA ATPase domain== | ||
<StructureSection load='5wc1' size='340' side='right' caption='[[5wc1]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='5wc1' size='340' side='right'caption='[[5wc1]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5wc1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WC1 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5wc1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WC1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5wc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wc1 OCA], [https://pdbe.org/5wc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wc1 RCSB], [https://www.ebi.ac.uk/pdbsum/5wc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wc1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KTNA1_CAEEL KTNA1_CAEEL] Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays. Required specifically for meiotic spindle formation in the female germline; the presence of this protein is inimical to the formation of mitotic spindles (PubMed:8027178, PubMed:10809666, PubMed:12885567). In body wall muscles, regulates organization of myosin thick filaments (PubMed:22621901).[HAMAP-Rule:MF_03023]<ref>PMID:10809666</ref> <ref>PMID:12885567</ref> <ref>PMID:22621901</ref> <ref>PMID:8027178</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Caenorhabditis elegans]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Roll-Mecak A]] | ||
[[Category: | [[Category: Szyk A]] | ||
Latest revision as of 17:10, 4 October 2023
katanin AAA ATPase domainkatanin AAA ATPase domain
Structural highlights
FunctionKTNA1_CAEEL Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays. Required specifically for meiotic spindle formation in the female germline; the presence of this protein is inimical to the formation of mitotic spindles (PubMed:8027178, PubMed:10809666, PubMed:12885567). In body wall muscles, regulates organization of myosin thick filaments (PubMed:22621901).[HAMAP-Rule:MF_03023][1] [2] [3] [4] Publication Abstract from PubMedMicrotubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing. Katanin spiral and ring structures shed light on power stroke for microtubule severing.,Zehr E, Szyk A, Piszczek G, Szczesna E, Zuo X, Roll-Mecak A Nat Struct Mol Biol. 2017 Aug 7. doi: 10.1038/nsmb.3448. PMID:28783150[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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