Role of Ca 2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin
A C a 2+ ‐dependent 1.5‐ MD a antifreeze protein present in an Antarctic Gram‐negative bacterium, M arinomonas primoryensis ( Mp AFP ), has recently been reassessed as an ice‐binding adhesin. The non‐ice‐binding region II ( RII ), one of five distinct domains in Mp AFP , constitutes ~ 90% of the pro...
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crwiley:10.1111/febs.12518 2024-06-02T07:57:53+00:00 Role of Ca 2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin Guo, Shuaiqi Garnham, Christopher P. Karunan Partha, Sarathy Campbell, Robert L. Allingham, John S. Davies, Peter L. 2013 http://dx.doi.org/10.1111/febs.12518 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Ffebs.12518 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.12518 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor The FEBS Journal volume 280, issue 22, page 5919-5932 ISSN 1742-464X 1742-4658 journal-article 2013 crwiley https://doi.org/10.1111/febs.12518 2024-05-03T11:13:18Z A C a 2+ ‐dependent 1.5‐ MD a antifreeze protein present in an Antarctic Gram‐negative bacterium, M arinomonas primoryensis ( Mp AFP ), has recently been reassessed as an ice‐binding adhesin. The non‐ice‐binding region II ( RII ), one of five distinct domains in Mp AFP , constitutes ~ 90% of the protein. RII consists of ~ 120 tandem copies of an identical 104‐residue sequence. We used the Protein Homology/analogy Recognition Engine server to define the boundaries of a single 104‐residue RII construct ( RII monomer). CD demonstrated that Ca 2+ is required for RII monomer folding, and that the monomer is fully structured at a Ca 2+ /protein molar ratio of 10 : 1. The crystal structure of the RII monomer was solved to a resolution of 1.35 Å by single‐wavelength anomalous dispersion and molecular replacement methods with Ca 2+ as the heavy atom to obtain phase information. The RII monomer folds as a Ca 2+ ‐bound immunoglobulin‐like β‐sandwich. Ca 2+ ions are coordinated at the interfaces between each RII monomer and its symmetry‐related molecules, suggesting that these ions may be involved in the stabilization of the tandemly repeated RII . We hypothesize that > 600 Ca 2+ ions help to rigidify the chain of 104‐residue repeats in order to project the ice‐binding domain of Mp AFP away from the bacterial cell surface. The proposed role of RII is to help the strictly aerobic bacterium bind surface ice in an Antarctic lake for better access to oxygen and nutrients. This work may give insights into other bacterial proteins that resemble Mp AFP , especially those of the large repeats‐in‐toxin family that have been characterized as adhesins exported via the type I secretion pathway. Database Structural data are available in the Protein Data Bank under the accession numbers 4KDW (P1 structure) and 4KDV (P2 1 structure). Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Antarctic The FEBS Journal 280 22 5919 5932 |
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Wiley Online Library |
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language |
English |
description |
A C a 2+ ‐dependent 1.5‐ MD a antifreeze protein present in an Antarctic Gram‐negative bacterium, M arinomonas primoryensis ( Mp AFP ), has recently been reassessed as an ice‐binding adhesin. The non‐ice‐binding region II ( RII ), one of five distinct domains in Mp AFP , constitutes ~ 90% of the protein. RII consists of ~ 120 tandem copies of an identical 104‐residue sequence. We used the Protein Homology/analogy Recognition Engine server to define the boundaries of a single 104‐residue RII construct ( RII monomer). CD demonstrated that Ca 2+ is required for RII monomer folding, and that the monomer is fully structured at a Ca 2+ /protein molar ratio of 10 : 1. The crystal structure of the RII monomer was solved to a resolution of 1.35 Å by single‐wavelength anomalous dispersion and molecular replacement methods with Ca 2+ as the heavy atom to obtain phase information. The RII monomer folds as a Ca 2+ ‐bound immunoglobulin‐like β‐sandwich. Ca 2+ ions are coordinated at the interfaces between each RII monomer and its symmetry‐related molecules, suggesting that these ions may be involved in the stabilization of the tandemly repeated RII . We hypothesize that > 600 Ca 2+ ions help to rigidify the chain of 104‐residue repeats in order to project the ice‐binding domain of Mp AFP away from the bacterial cell surface. The proposed role of RII is to help the strictly aerobic bacterium bind surface ice in an Antarctic lake for better access to oxygen and nutrients. This work may give insights into other bacterial proteins that resemble Mp AFP , especially those of the large repeats‐in‐toxin family that have been characterized as adhesins exported via the type I secretion pathway. Database Structural data are available in the Protein Data Bank under the accession numbers 4KDW (P1 structure) and 4KDV (P2 1 structure). |
format |
Article in Journal/Newspaper |
author |
Guo, Shuaiqi Garnham, Christopher P. Karunan Partha, Sarathy Campbell, Robert L. Allingham, John S. Davies, Peter L. |
spellingShingle |
Guo, Shuaiqi Garnham, Christopher P. Karunan Partha, Sarathy Campbell, Robert L. Allingham, John S. Davies, Peter L. Role of Ca 2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin |
author_facet |
Guo, Shuaiqi Garnham, Christopher P. Karunan Partha, Sarathy Campbell, Robert L. Allingham, John S. Davies, Peter L. |
author_sort |
Guo, Shuaiqi |
title |
Role of Ca 2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin |
title_short |
Role of Ca 2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin |
title_full |
Role of Ca 2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin |
title_fullStr |
Role of Ca 2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin |
title_full_unstemmed |
Role of Ca 2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin |
title_sort |
role of ca 2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin |
publisher |
Wiley |
publishDate |
2013 |
url |
http://dx.doi.org/10.1111/febs.12518 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Ffebs.12518 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.12518 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
The FEBS Journal volume 280, issue 22, page 5919-5932 ISSN 1742-464X 1742-4658 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/febs.12518 |
container_title |
The FEBS Journal |
container_volume |
280 |
container_issue |
22 |
container_start_page |
5919 |
op_container_end_page |
5932 |
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1800741093549015040 |