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| | <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 [http://proteopedia.org/fgij/fg.htm?mol=5WC1 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Microtubule-severing_ATPase Microtubule-severing ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.3 3.6.4.3] </span></td></tr> | + | <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'>[http://proteopedia.org/fgij/fg.htm?mol=5wc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wc1 OCA], [http://pdbe.org/5wc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5wc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wc1 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=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 == |
| - | [[http://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> | + | [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: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Microtubule-severing ATPase]]
| + | [[Category: Roll-Mecak A]] |
| - | [[Category: Roll-Mecak, A]] | + | [[Category: Szyk A]] |
| - | [[Category: Szyk, A]] | + | |
| - | [[Category: Cytosolic protein]]
| + | |
| - | [[Category: Microtubule severing enzyme]]
| + | |
| Structural highlights
Function
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][1] [2] [3] [4]
Publication Abstract from PubMed
Microtubule-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
- ↑ Srayko M, Buster DW, Bazirgan OA, McNally FJ, Mains PE. MEI-1/MEI-2 katanin-like microtubule severing activity is required for Caenorhabditis elegans meiosis. Genes Dev. 2000 May 1;14(9):1072-84. PMID:10809666
- ↑ Yang HY, McNally K, McNally FJ. MEI-1/katanin is required for translocation of the meiosis I spindle to the oocyte cortex in C elegans. Dev Biol. 2003 Aug 1;260(1):245-59. PMID:12885567
- ↑ Wilson KJ, Qadota H, Mains PE, Benian GM. UNC-89 (obscurin) binds to MEL-26, a BTB-domain protein, and affects the function of MEI-1 (katanin) in striated muscle of Caenorhabditis elegans. Mol Biol Cell. 2012 Jul;23(14):2623-34. doi: 10.1091/mbc.E12-01-0055. Epub 2012, May 23. PMID:22621901 doi:http://dx.doi.org/10.1091/mbc.E12-01-0055
- ↑ Clark-Maguire S, Mains PE. Localization of the mei-1 gene product of Caenorhaditis elegans, a meiotic-specific spindle component. J Cell Biol. 1994 Jul;126(1):199-209. PMID:8027178
- ↑ Zehr E, Szyk A, Piszczek G, Szczesna E, Zuo X, Roll-Mecak A. Katanin spiral and ring structures shed light on power stroke for microtubule severing. Nat Struct Mol Biol. 2017 Aug 7. doi: 10.1038/nsmb.3448. PMID:28783150 doi:http://dx.doi.org/10.1038/nsmb.3448
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