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| | <SX load='5kyh' size='340' side='right' viewer='molstar' caption='[[5kyh]], [[Resolution|resolution]] 4.00Å' scene=''> | | <SX load='5kyh' size='340' side='right' viewer='molstar' caption='[[5kyh]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5kyh]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_18386 Dsm 18386]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KYH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KYH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5kyh]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Ignicoccus_hospitalis Ignicoccus hospitalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KYH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j1r|3j1r]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Igni_0670 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160233 DSM 18386])</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=5kyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kyh OCA], [https://pdbe.org/5kyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kyh RCSB], [https://www.ebi.ac.uk/pdbsum/5kyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kyh ProSAT]</span></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=5kyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kyh OCA], [http://pdbe.org/5kyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kyh RCSB], [http://www.ebi.ac.uk/pdbsum/5kyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kyh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A8AAA0_IGNH4 A8AAA0_IGNH4] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Dsm 18386]] | + | [[Category: Ignicoccus hospitalis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Braun, T]] | + | [[Category: Braun T]] |
| - | [[Category: Egelman, E H]] | + | [[Category: Egelman EH]] |
| - | [[Category: Kalisman, N]] | + | [[Category: Kalisman N]] |
| - | [[Category: Rachel, R]] | + | [[Category: Rachel R]] |
| - | [[Category: Schroeder, G F]] | + | [[Category: Schroeder GF]] |
| - | [[Category: Sherman, N E]] | + | [[Category: Sherman NE]] |
| - | [[Category: Vos, M]] | + | [[Category: Vos M]] |
| - | [[Category: Wirth, R]] | + | [[Category: Wirth R]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Flagellin]]
| + | |
| - | [[Category: Immunoglobulin fold]]
| + | |
| - | [[Category: Type iv pili]]
| + | |
| Structural highlights
Function
A8AAA0_IGNH4
Publication Abstract from PubMed
The bacterial flagellar apparatus, which involves approximately 40 different proteins, has been a model system for understanding motility and chemotaxis. The bacterial flagellar filament, largely composed of a single protein, flagellin, has been a model for understanding protein assembly. This system has no homology to the eukaryotic flagellum, in which the filament alone, composed of a microtubule-based axoneme, contains more than 400 different proteins. The archaeal flagellar system is simpler still, in some cases having approximately 13 different proteins with a single flagellar filament protein. The archaeal flagellar system has no homology to the bacterial one and must have arisen by convergent evolution. However, it has been understood that the N-terminal domain of the archaeal flagellin is a homolog of the N-terminal domain of bacterial type IV pilin, showing once again how proteins can be repurposed in evolution for different functions. Using cryo-EM, we have been able to generate a nearly complete atomic model for a flagellar-like filament of the archaeon Ignicoccus hospitalis from a reconstruction at approximately 4-A resolution. We can now show that the archaeal flagellar filament contains a beta-sandwich, previously seen in the FlaF protein that forms the anchor for the archaeal flagellar filament. In contrast to the bacterial flagellar filament, where the outer globular domains make no contact with each other and are not necessary for either assembly or motility, the archaeal flagellin outer domains make extensive contacts with each other that largely determine the interesting mechanical properties of these filaments, allowing these filaments to flex.
Archaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain.,Braun T, Vos MR, Kalisman N, Sherman NE, Rachel R, Wirth R, Schroder GF, Egelman EH Proc Natl Acad Sci U S A. 2016 Aug 30. pii: 201607756. PMID:27578865[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Braun T, Vos MR, Kalisman N, Sherman NE, Rachel R, Wirth R, Schroder GF, Egelman EH. Archaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain. Proc Natl Acad Sci U S A. 2016 Aug 30. pii: 201607756. PMID:27578865 doi:http://dx.doi.org/10.1073/pnas.1607756113
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