7pnb: Difference between revisions
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==Sulfolobus acidocaldarius 0406 filament.== | |||
<StructureSection load='7pnb' size='340' side='right'caption='[[7pnb]], [[Resolution|resolution]] 3.46Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7pnb]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PNB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.46Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=YZT:6-deoxy-6-sulfo-beta-D-glucopyranose'>YZT</scene></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=7pnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pnb OCA], [https://pdbe.org/7pnb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pnb RCSB], [https://www.ebi.ac.uk/pdbsum/7pnb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pnb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4JBK8_SULAC Q4JBK8_SULAC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV pilus superfamily (archaella, archaeal adhesion pili and UV-inducible pili), as well as a so-far uncharacterised fourth filament, named "thread". Here, we report on the cryo-EM structure of the archaeal thread. The filament is highly glycosylated and consists of subunits of the protein Saci_0406, arranged in a head-to-tail manner. Saci_0406 displays structural similarity, but low sequence homology, to bacterial type-I pilins. Thread subunits are interconnected via donor strand complementation, a feature reminiscent of bacterial chaperone-usher pili. However, despite these similarities in overall architecture, archaeal threads appear to have evolved independently and are likely assembled by a distinct mechanism. | |||
Electron cryo-microscopy reveals the structure of the archaeal thread filament.,Gaines MC, Isupov MN, Sivabalasarma S, Haque RU, McLaren M, Mollat CL, Tripp P, Neuhaus A, Gold VAM, Albers SV, Daum B Nat Commun. 2022 Dec 1;13(1):7411. doi: 10.1038/s41467-022-34652-4. PMID:36456543<ref>PMID:36456543</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7pnb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sulfolobus acidocaldarius]] | |||
[[Category: Daum B]] | |||
[[Category: Gaines M]] | |||
[[Category: Isupov MN]] | |||
Latest revision as of 16:54, 6 November 2024
Sulfolobus acidocaldarius 0406 filament.Sulfolobus acidocaldarius 0406 filament.
Structural highlights
FunctionPublication Abstract from PubMedPili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV pilus superfamily (archaella, archaeal adhesion pili and UV-inducible pili), as well as a so-far uncharacterised fourth filament, named "thread". Here, we report on the cryo-EM structure of the archaeal thread. The filament is highly glycosylated and consists of subunits of the protein Saci_0406, arranged in a head-to-tail manner. Saci_0406 displays structural similarity, but low sequence homology, to bacterial type-I pilins. Thread subunits are interconnected via donor strand complementation, a feature reminiscent of bacterial chaperone-usher pili. However, despite these similarities in overall architecture, archaeal threads appear to have evolved independently and are likely assembled by a distinct mechanism. Electron cryo-microscopy reveals the structure of the archaeal thread filament.,Gaines MC, Isupov MN, Sivabalasarma S, Haque RU, McLaren M, Mollat CL, Tripp P, Neuhaus A, Gold VAM, Albers SV, Daum B Nat Commun. 2022 Dec 1;13(1):7411. doi: 10.1038/s41467-022-34652-4. PMID:36456543[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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