Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice
The large size of a 1.5-MDa ice-binding adhesin [MpAFP (Marinomonas primoryensis antifreeze protein)] from an Antarctic Gram-negative bacterium, M. primoryensis, is mainly due to its highly repetitive RII (Region II). MpAFP_RII contains roughly 120 tandem copies of an identical 104-residue repeat. W...
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Portland Press, Biochemical Society
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ftdoajarticles:oai:doaj.org/article:ceefbafa569c4aee81c7cb6c4bd211db 2023-05-15T13:32:48+02:00 Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice Tyler D. R. Vance Luuk L. C. Olijve Robert L. Campbell Ilja K. Voets Peter L. Davies Shuaiqi Guo 2014-07-01T00:00:00Z https://doi.org/10.1042/BSR20140083 https://doaj.org/article/ceefbafa569c4aee81c7cb6c4bd211db EN eng Portland Press, Biochemical Society http://www.bioscirep.org/bsr/034/e121/bsr034e121.htm https://doaj.org/toc/1573-4935 1573-4935 doi:10.1042/BSR20140083 https://doaj.org/article/ceefbafa569c4aee81c7cb6c4bd211db Bioscience Reports, Vol 34, Iss 4, p e00121 (2014) bacterial Ig-like fold Ca2+-binding crystal structure extender domain ice-binding adhesin solution structure Life QH501-531 Microbiology QR1-502 article 2014 ftdoajarticles https://doi.org/10.1042/BSR20140083 2022-12-31T12:59:13Z The large size of a 1.5-MDa ice-binding adhesin [MpAFP (Marinomonas primoryensis antifreeze protein)] from an Antarctic Gram-negative bacterium, M. primoryensis, is mainly due to its highly repetitive RII (Region II). MpAFP_RII contains roughly 120 tandem copies of an identical 104-residue repeat. We have previously determined that a single RII repeat folds as a Ca2+-dependent immunoglobulin-like domain. Here, we solved the crystal structure of RII tetra-tandemer (four tandem RII repeats) to a resolution of 1.8 Å. The RII tetra-tandemer reveals an extended (~190-Å × ~25-Å), rod-like structure with four RII-repeats aligned in series with each other. The inter-repeat regions of the RII tetra-tandemer are strengthened by Ca2+ bound to acidic residues. SAXS (small-angle X-ray scattering) profiles indicate the RII tetra-tandemer is significantly rigidified upon Ca2+ binding, and that the protein's solution structure is in excellent agreement with its crystal structure. We hypothesize that >600 Ca2+ help rigidify the chain of ~120 104-residue repeats to form a ~0.6 μm rod-like structure in order to project the ice-binding domain of MpAFP away from the bacterial cell surface. The proposed extender role of RII can help the strictly aerobic, motile bacterium bind ice in the upper reaches of the Antarctic lake where oxygen and nutrients are most abundant. Ca2+-induced rigidity of tandem Ig-like repeats in large adhesins might be a general mechanism used by bacteria to bind to their substrates and help colonize specific niches. Article in Journal/Newspaper Antarc* Antarctic Directory of Open Access Journals: DOAJ Articles Antarctic The Antarctic Bioscience Reports 34 4 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
bacterial Ig-like fold Ca2+-binding crystal structure extender domain ice-binding adhesin solution structure Life QH501-531 Microbiology QR1-502 |
spellingShingle |
bacterial Ig-like fold Ca2+-binding crystal structure extender domain ice-binding adhesin solution structure Life QH501-531 Microbiology QR1-502 Tyler D. R. Vance Luuk L. C. Olijve Robert L. Campbell Ilja K. Voets Peter L. Davies Shuaiqi Guo Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice |
topic_facet |
bacterial Ig-like fold Ca2+-binding crystal structure extender domain ice-binding adhesin solution structure Life QH501-531 Microbiology QR1-502 |
description |
The large size of a 1.5-MDa ice-binding adhesin [MpAFP (Marinomonas primoryensis antifreeze protein)] from an Antarctic Gram-negative bacterium, M. primoryensis, is mainly due to its highly repetitive RII (Region II). MpAFP_RII contains roughly 120 tandem copies of an identical 104-residue repeat. We have previously determined that a single RII repeat folds as a Ca2+-dependent immunoglobulin-like domain. Here, we solved the crystal structure of RII tetra-tandemer (four tandem RII repeats) to a resolution of 1.8 Å. The RII tetra-tandemer reveals an extended (~190-Å × ~25-Å), rod-like structure with four RII-repeats aligned in series with each other. The inter-repeat regions of the RII tetra-tandemer are strengthened by Ca2+ bound to acidic residues. SAXS (small-angle X-ray scattering) profiles indicate the RII tetra-tandemer is significantly rigidified upon Ca2+ binding, and that the protein's solution structure is in excellent agreement with its crystal structure. We hypothesize that >600 Ca2+ help rigidify the chain of ~120 104-residue repeats to form a ~0.6 μm rod-like structure in order to project the ice-binding domain of MpAFP away from the bacterial cell surface. The proposed extender role of RII can help the strictly aerobic, motile bacterium bind ice in the upper reaches of the Antarctic lake where oxygen and nutrients are most abundant. Ca2+-induced rigidity of tandem Ig-like repeats in large adhesins might be a general mechanism used by bacteria to bind to their substrates and help colonize specific niches. |
format |
Article in Journal/Newspaper |
author |
Tyler D. R. Vance Luuk L. C. Olijve Robert L. Campbell Ilja K. Voets Peter L. Davies Shuaiqi Guo |
author_facet |
Tyler D. R. Vance Luuk L. C. Olijve Robert L. Campbell Ilja K. Voets Peter L. Davies Shuaiqi Guo |
author_sort |
Tyler D. R. Vance |
title |
Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice |
title_short |
Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice |
title_full |
Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice |
title_fullStr |
Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice |
title_full_unstemmed |
Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice |
title_sort |
ca2+-stabilized adhesin helps an antarctic bacterium reach out and bind ice |
publisher |
Portland Press, Biochemical Society |
publishDate |
2014 |
url |
https://doi.org/10.1042/BSR20140083 https://doaj.org/article/ceefbafa569c4aee81c7cb6c4bd211db |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Bioscience Reports, Vol 34, Iss 4, p e00121 (2014) |
op_relation |
http://www.bioscirep.org/bsr/034/e121/bsr034e121.htm https://doaj.org/toc/1573-4935 1573-4935 doi:10.1042/BSR20140083 https://doaj.org/article/ceefbafa569c4aee81c7cb6c4bd211db |
op_doi |
https://doi.org/10.1042/BSR20140083 |
container_title |
Bioscience Reports |
container_volume |
34 |
container_issue |
4 |
_version_ |
1766035925097250816 |