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| | ==Cryo-EM structure of Methanoccus maripaludis archaellum== | | ==Cryo-EM structure of Methanoccus maripaludis archaellum== |
| - | <StructureSection load='5z1l' size='340' side='right'caption='[[5z1l]], [[Resolution|resolution]] 4.00Å' scene=''> | + | <SX load='5z1l' size='340' side='right' viewer='molstar' caption='[[5z1l]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5z1l]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Metmp Metmp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z1L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5z1l]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanococcus_maripaludis_S2 Methanococcus maripaludis S2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z1L FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1arc|1arc]]</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]] 4Å</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=5z1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z1l OCA], [http://pdbe.org/5z1l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z1l RCSB], [http://www.ebi.ac.uk/pdbsum/5z1l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z1l 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=5z1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z1l OCA], [https://pdbe.org/5z1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z1l RCSB], [https://www.ebi.ac.uk/pdbsum/5z1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z1l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q6LWP3_METMP Q6LWP3_METMP]] Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.[RuleBase:RU361282] | + | [https://www.uniprot.org/uniprot/Q6LWP3_METMP Q6LWP3_METMP] Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.[RuleBase:RU361282] |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Many archaea swim by means of archaella. While the archaellum is similar in function to its bacterial counterpart, its structure, composition, and evolution are fundamentally different. Archaella are related to archaeal and bacterial type IV pili. Despite recent advances, our understanding of molecular processes governing archaellum assembly and stability is still incomplete. Here, we determine the structures of Methanococcus archaella by X-ray crystallography and cryo-EM The crystal structure of Methanocaldococcus jannaschii FlaB1 is the first and only crystal structure of any archaellin to date at a resolution of 1.5 A, which is put into biological context by a cryo-EM reconstruction from Methanococcus maripaludis archaella at 4 A resolution created with helical single-particle analysis. Our results indicate that the archaellum is predominantly composed of FlaB1. We identify N-linked glycosylation by cryo-EM and mass spectrometry. The crystal structure reveals a highly conserved metal-binding site, which is validated by mass spectrometry and electron energy-loss spectroscopy. We show in vitro that the metal-binding site, which appears to be a widespread property of archaellin, is required for filament integrity.
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| - | High-resolution archaellum structure reveals a conserved metal-binding site.,Meshcheryakov VA, Shibata S, Schreiber MT, Villar-Briones A, Jarrell KF, Aizawa SI, Wolf M EMBO Rep. 2019 Mar 21. pii: embr.201846340. doi: 10.15252/embr.201846340. PMID:30898768<ref>PMID:30898768</ref>
| + | ==See Also== |
| - | | + | *[[Flagellin 3D structures|Flagellin 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 5z1l" style="background-color:#fffaf0;"></div>
| + | |
| - | == References == | + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metmp]] | + | [[Category: Methanococcus maripaludis S2]] |
| - | [[Category: Aizawa, S]] | + | [[Category: Aizawa S]] |
| - | [[Category: Jarrell, K F]] | + | [[Category: Jarrell KF]] |
| - | [[Category: Meshcheryakov, V A]] | + | [[Category: Meshcheryakov VA]] |
| - | [[Category: Schreiber, M T]] | + | [[Category: Schreiber MT]] |
| - | [[Category: Shibata, S]] | + | [[Category: Shibata S]] |
| - | [[Category: Villar-Briones, A]] | + | [[Category: Villar-Briones A]] |
| - | [[Category: Wolf, M]] | + | [[Category: Wolf M]] |
| - | [[Category: Archaellum]]
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| - | [[Category: Archea]]
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| - | [[Category: Flagellum]]
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| - | [[Category: Helical]]
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| - | [[Category: Metal binding]]
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| - | [[Category: Motility]]
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| - | [[Category: Protein fibril]]
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