Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice
Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium Marinomonas primoryensis uses a 1.5-MDa adhesin comprising over 130 domains to position it on ice at the top of the water column for better access to oxygen and...
Published in: | Science Advances |
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ftuniveindcris:oai:pure.tue.nl:publications/a68617e0-427b-4438-8eb2-4e9272c91de8 2024-06-23T07:47:49+00:00 Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice Guo, S. Stevens, C.A. Vance, T.D.R. Olijve, L.L.C. Graham, L.A. Campbell, R.L. Yazdi, S.R. Escobedo, C. Bar-Dolev, M. Yashunsky, V. Braslavsky, I. Langelaan, D.N. Smith, S.P. Allingham, J.S. Voets, I.K. Davies, P.L. 2017-08 application/pdf https://research.tue.nl/en/publications/a68617e0-427b-4438-8eb2-4e9272c91de8 https://doi.org/10.1126/sciadv.1701440 https://pure.tue.nl/ws/files/91221056/guostruc2017.pdf eng eng https://research.tue.nl/en/publications/a68617e0-427b-4438-8eb2-4e9272c91de8 info:eu-repo/semantics/openAccess Guo , S , Stevens , C A , Vance , T D R , Olijve , L L C , Graham , L A , Campbell , R L , Yazdi , S R , Escobedo , C , Bar-Dolev , M , Yashunsky , V , Braslavsky , I , Langelaan , D N , Smith , S P , Allingham , J S , Voets , I K & Davies , P L 2017 , ' Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice ' , Science Advances , vol. 3 , no. 8 , e1701440 , pp. 1-10 . https://doi.org/10.1126/sciadv.1701440 Adhesins Bacterial/chemistry Amino Acid Sequence Antarctic Regions Bacteria/metabolism Binding Sites Biofilms Diatoms/microbiology Ice Cover/microbiology Ligands Models Biological Molecular Protein Conformation Protein Interaction Domains and Motifs Structure-Activity Relationship Symbiosis Type I Secretion Systems/genetics article 2017 ftuniveindcris https://doi.org/10.1126/sciadv.1701440 2024-06-12T23:56:33Z Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium Marinomonas primoryensis uses a 1.5-MDa adhesin comprising over 130 domains to position it on ice at the top of the water column for better access to oxygen and nutrients. We have reconstructed this 0.6-μm-long adhesin using a “dissect and build” structural biology approach and have established complementary roles for its five distinct regions. Domains in region I (RI) tether the adhesin to the type I secretion machinery in the periplasm of the bacterium and pass it through the outer membrane. RII comprises ~120 identical immunoglobulin-like β-sandwich domains that rigidify on binding Ca2+ to project the adhesion regions RIII and RIV into the medium. RIII contains ligand-binding domains that join diatoms and bacteria together in a mixed-species community on the underside of sea ice where incident light is maximal. RIV is the ice-binding domain, and the terminal RV domain contains several “repeats-in-toxin” motifs and a noncleavable signal sequence that target proteins for export via the type I secretion system. Similar structural architecture is present in the adhesins of many pathogenic bacteria and provides a guide to finding and blocking binding domains to weaken infectivity. Article in Journal/Newspaper Antarc* Antarctic Sea ice Eindhoven University of Technology research portal Antarctic The Antarctic Science Advances 3 8 |
institution |
Open Polar |
collection |
Eindhoven University of Technology research portal |
op_collection_id |
ftuniveindcris |
language |
English |
topic |
Adhesins Bacterial/chemistry Amino Acid Sequence Antarctic Regions Bacteria/metabolism Binding Sites Biofilms Diatoms/microbiology Ice Cover/microbiology Ligands Models Biological Molecular Protein Conformation Protein Interaction Domains and Motifs Structure-Activity Relationship Symbiosis Type I Secretion Systems/genetics |
spellingShingle |
Adhesins Bacterial/chemistry Amino Acid Sequence Antarctic Regions Bacteria/metabolism Binding Sites Biofilms Diatoms/microbiology Ice Cover/microbiology Ligands Models Biological Molecular Protein Conformation Protein Interaction Domains and Motifs Structure-Activity Relationship Symbiosis Type I Secretion Systems/genetics Guo, S. Stevens, C.A. Vance, T.D.R. Olijve, L.L.C. Graham, L.A. Campbell, R.L. Yazdi, S.R. Escobedo, C. Bar-Dolev, M. Yashunsky, V. Braslavsky, I. Langelaan, D.N. Smith, S.P. Allingham, J.S. Voets, I.K. Davies, P.L. Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice |
topic_facet |
Adhesins Bacterial/chemistry Amino Acid Sequence Antarctic Regions Bacteria/metabolism Binding Sites Biofilms Diatoms/microbiology Ice Cover/microbiology Ligands Models Biological Molecular Protein Conformation Protein Interaction Domains and Motifs Structure-Activity Relationship Symbiosis Type I Secretion Systems/genetics |
description |
Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium Marinomonas primoryensis uses a 1.5-MDa adhesin comprising over 130 domains to position it on ice at the top of the water column for better access to oxygen and nutrients. We have reconstructed this 0.6-μm-long adhesin using a “dissect and build” structural biology approach and have established complementary roles for its five distinct regions. Domains in region I (RI) tether the adhesin to the type I secretion machinery in the periplasm of the bacterium and pass it through the outer membrane. RII comprises ~120 identical immunoglobulin-like β-sandwich domains that rigidify on binding Ca2+ to project the adhesion regions RIII and RIV into the medium. RIII contains ligand-binding domains that join diatoms and bacteria together in a mixed-species community on the underside of sea ice where incident light is maximal. RIV is the ice-binding domain, and the terminal RV domain contains several “repeats-in-toxin” motifs and a noncleavable signal sequence that target proteins for export via the type I secretion system. Similar structural architecture is present in the adhesins of many pathogenic bacteria and provides a guide to finding and blocking binding domains to weaken infectivity. |
format |
Article in Journal/Newspaper |
author |
Guo, S. Stevens, C.A. Vance, T.D.R. Olijve, L.L.C. Graham, L.A. Campbell, R.L. Yazdi, S.R. Escobedo, C. Bar-Dolev, M. Yashunsky, V. Braslavsky, I. Langelaan, D.N. Smith, S.P. Allingham, J.S. Voets, I.K. Davies, P.L. |
author_facet |
Guo, S. Stevens, C.A. Vance, T.D.R. Olijve, L.L.C. Graham, L.A. Campbell, R.L. Yazdi, S.R. Escobedo, C. Bar-Dolev, M. Yashunsky, V. Braslavsky, I. Langelaan, D.N. Smith, S.P. Allingham, J.S. Voets, I.K. Davies, P.L. |
author_sort |
Guo, S. |
title |
Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice |
title_short |
Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice |
title_full |
Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice |
title_fullStr |
Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice |
title_full_unstemmed |
Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice |
title_sort |
structure of a 1.5-mda adhesin that binds its antarctic bacterium to diatoms and ice |
publishDate |
2017 |
url |
https://research.tue.nl/en/publications/a68617e0-427b-4438-8eb2-4e9272c91de8 https://doi.org/10.1126/sciadv.1701440 https://pure.tue.nl/ws/files/91221056/guostruc2017.pdf |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Sea ice |
genre_facet |
Antarc* Antarctic Sea ice |
op_source |
Guo , S , Stevens , C A , Vance , T D R , Olijve , L L C , Graham , L A , Campbell , R L , Yazdi , S R , Escobedo , C , Bar-Dolev , M , Yashunsky , V , Braslavsky , I , Langelaan , D N , Smith , S P , Allingham , J S , Voets , I K & Davies , P L 2017 , ' Structure of a 1.5-MDa adhesin that binds its antarctic bacterium to diatoms and ice ' , Science Advances , vol. 3 , no. 8 , e1701440 , pp. 1-10 . https://doi.org/10.1126/sciadv.1701440 |
op_relation |
https://research.tue.nl/en/publications/a68617e0-427b-4438-8eb2-4e9272c91de8 |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1126/sciadv.1701440 |
container_title |
Science Advances |
container_volume |
3 |
container_issue |
8 |
_version_ |
1802637999146532864 |