Structure of the two-component S-layer of the archaeon Sulfolobus acidocaldarius
dc.contributor.author | Gambelli, L | |
dc.contributor.author | McLaren, M | |
dc.contributor.author | Conners, R | |
dc.contributor.author | Sanders, K | |
dc.contributor.author | Gaines, MC | |
dc.contributor.author | Clark, L | |
dc.contributor.author | Gold, VAM | |
dc.contributor.author | Kattnig, D | |
dc.contributor.author | Sikora, M | |
dc.contributor.author | Hanus, C | |
dc.contributor.author | Isupov, MN | |
dc.contributor.author | Daum, B | |
dc.date.accessioned | 2024-01-29T10:06:11Z | |
dc.date.issued | 2024-01-22 | |
dc.date.updated | 2024-01-27T08:57:07Z | |
dc.description.abstract | Surface layers (S-layers) are resilient two-dimensional protein lattices that encapsulate many bacteria and most archaea. In archaea, S-layers usually form the only structural component of the cell wall and thus act as the final frontier between the cell and its environment. Therefore, S-layers are crucial for supporting microbial life. Notwithstanding their importance, little is known about archaeal S-layers at the atomic level. Here, we combined single particle cryo electron microscopy (cryoEM), cryo electron tomography (cryoET) and Alphafold2 predictions to generate an atomic model of the two-component S-layer of Sulfolobus acidocaldarius. The outer component of this S-layer (SlaA) is a flexible, highly glycosylated, and stable protein. Together with the inner and membrane-bound component (SlaB), they assemble into a porous and interwoven lattice. We hypothesise that jackknife-like conformational changes, changes play important roles in S-layer assembly. | en_GB |
dc.description.sponsorship | European Research Council | en_GB |
dc.description.sponsorship | Wellcome Trust | en_GB |
dc.description.sponsorship | Wellcome Trust | en_GB |
dc.description.sponsorship | Agence Nationale de la Recherche | en_GB |
dc.description.sponsorship | Agence Nationale de la Recherche | en_GB |
dc.description.sponsorship | Leverhulme Trust | en_GB |
dc.description.sponsorship | Biotechnology and Biological Sciences Research Council (BBSRC) | en_GB |
dc.identifier.citation | Published online 22 January 2024 | en_GB |
dc.identifier.doi | https://doi.org/10.7554/elife.84617 | |
dc.identifier.grantnumber | 803894 | en_GB |
dc.identifier.grantnumber | 210363/Z/18/Z | en_GB |
dc.identifier.grantnumber | 212439/Z/18/Z | en_GB |
dc.identifier.grantnumber | ANR-16-CE16-0009-01 | en_GB |
dc.identifier.grantnumber | ANR-21-CE16-0021-01 | en_GB |
dc.identifier.grantnumber | RPG-2020-261 | en_GB |
dc.identifier.grantnumber | BB/R008639/1 | en_GB |
dc.identifier.uri | http://hdl.handle.net/10871/135176 | |
dc.identifier | ORCID: 0000-0002-6908-0745 (Gold, Vicki AM) | |
dc.identifier | ORCID: 0000-0002-3767-264X (Daum, Bertram) | |
dc.language.iso | en | en_GB |
dc.publisher | eLife Sciences Publications | en_GB |
dc.relation.url | https://www.rcsb.org/ | en_GB |
dc.relation.url | https://www.emdataresource.org/ | en_GB |
dc.relation.url | http://dx.doi.org/10.2210/pdb7ptr/pdb | en_GB |
dc.relation.url | http://dx.doi.org/10.2210/pdb6t72/pdb | en_GB |
dc.relation.url | http://dx.doi.org/10.2210/pdb5n8p/pdb | en_GB |
dc.rights | © 2024, Gambelli et al. This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited. Metrics | en_GB |
dc.title | Structure of the two-component S-layer of the archaeon Sulfolobus acidocaldarius | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2024-01-29T10:06:11Z | |
dc.description | This is the author accepted manuscript. The final version is available from eLife Sciences Publications via the DOI in this record | en_GB |
dc.description | Data availability: The atomic coordinates of SlaA were deposited in the Protein Data Bank (https://www.rcsb.org/) with accession numbers PDB-7ZCX, PDDB-8AN3, and PDB-8AN3 for pH 4, 7 and 10, respectively. The electron density maps were deposited in the EM DataResource (https://www.emdataresource.org/) with accession numbers EMD-14635, EMD-15531 and EMD-15531 for pH 4, 7 and 10, respectively. Sub-tomogram averaging map of the S-layer has been deposited in the EMDB (EMD-18127) and models of the hexameric and trimeric pores in the Protein Databank under accession codes PDB-8QP0 and PDB-8QOX, respectivelyOther structural data used in this study are: H. volcanii csg (PDB ID: 7PTR, http://dx.doi.org/10.2210/pdb7ptr/pdb), and C. crescentus RsaA ((N-terminus PDB ID: 6T72, http://dx.doi.org/10.2210/pdb6t72/pdb, C-terminus PDB ID: 5N8P, http://dx.doi.org/10.2210/pdb5n8p/pdb). | en_GB |
dc.identifier.eissn | 2050-084X | |
dc.identifier.journal | eLife | en_GB |
dc.relation.ispartof | eLife, 13 | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | en_GB |
dcterms.dateAccepted | 2024-01-19 | |
rioxxterms.version | VoR | en_GB |
rioxxterms.licenseref.startdate | 2024-01-19 | |
rioxxterms.type | Journal Article/Review | en_GB |
refterms.dateFCD | 2024-01-29T10:02:10Z | |
refterms.versionFCD | VoR | |
refterms.dateFOA | 2024-01-29T10:06:41Z | |
refterms.panel | A | en_GB |
refterms.dateFirstOnline | 2024-01-22 |
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