This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5wcb

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Katanin hexamer in the ring conformation

5wcb, resolution 6.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5wcb"

@@ Line 3: / Line 3: @@
 <SX load='5wcb' size='340' side='right' viewer='molstar' caption='[[5wcb]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5wcb]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WCB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WCB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5wcb]] is a 6 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=5WCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WCB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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]] 6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wc0|5wc0]], [[5wc1|5wc1]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mei-1, T01G9.5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=5wcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wcb OCA], [https://pdbe.org/5wcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wcb RCSB], [https://www.ebi.ac.uk/pdbsum/5wcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wcb ProSAT]</span></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='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=5wcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wcb OCA], [http://pdbe.org/5wcb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wcb RCSB], [http://www.ebi.ac.uk/pdbsum/5wcb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wcb ProSAT]</span></td></tr>
 </table>
 == 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;">
-== 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<ref>PMID:28783150</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5wcb" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Caeel]]
+[[Category: Caenorhabditis elegans]]
 [[Category: Large Structures]]
-[[Category: Microtubule-severing ATPase]]
+[[Category: Piszczek G]]
-[[Category: Piszczek, G]]
+[[Category: Roll-Mecak A]]
-[[Category: Roll-Mecak, A]]
+[[Category: Szczesna E]]
-[[Category: Szczesna, E]]
+[[Category: Szyk A]]
-[[Category: Szyk, A]]
+[[Category: Zehr EA]]
-[[Category: Zehr, E A]]
+[[Category: Zuo X]]
-[[Category: Zuo, X]]
-[[Category: Aaa atpase]]
-[[Category: Microtubule cytoskeleton]]
-[[Category: Microtubule severing protein]]
-[[Category: Motor protein]]
-[[Category: P60]]

5wcb

From Proteopedia

Current revision

Katanin hexamer in the ring conformation

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox