Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice.
Open accessAbstract
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.
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Each of the four chains of the 4p99 structure contains four fibronectin-like domains surrounded by calcium ions.
“Each of the four chains contain four fibronectin like domains surrounded by calcium ions (Vance et al., 2014).”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Vance et al., 2014
The Results section (“Crystal structure of RII tetra-tandemer”) reports four copies of the structure, each containing four Ca2+-binding repeats. It identifies those repeats as Ig-like β-sandwich domains, not fibronectin-like domains; our copy also does not identify the structure by the code 4p99. (LLM, conf=0.88)
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- Authors
- Vance, T. D. R., Olijve, L. L. C., Campbell, R. L., Voets, I. K., Davies, P. L., & Guo, S.
- Affiliations
- Queen's University (CA)
- Eindhoven University of Technology (NL)
- Corresponding author
- Guo, Shuaiqi
- ORCID
- Venue
- Bioscience Reports
- Publisher
- Portland Press Ltd.
- Published
- 2014-07-04
- Volume
- 34
- Issue
- 4
- ISSN
- 0144-8463 (ISSN-L)
- 1573-4935
- PMC
- PMC4083281
- OpenAlex
- W1967799249
- Cited by
- 40
- References
- 47
- Citations by year
- 2025: 3 · 2024: 4 · 2023: 1 · 2022: 4 · 2020: 8 · 2019: 3 · 2018: 3 · 2017: 6 · 2016: 5 · 2015: 2 · 2014: 1
- FWCI
- 1.91
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Bioscience Reports (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- TU/e Research Portal (submittedVersion, cc-by)
- TU/e Research Portal (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- European Commission (FP7-PEOPLE-2011, 293788, FP7-PEOPLE-2011-CIG)
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (700.10.406)
- Queen's University
- Canadian Institutes of Health Research
- Brookhaven National Laboratory
- FP7 People: Marie-Curie Actions
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Physical Sciences › Environmental Science › Ecology › Polar Research and Ecology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- antifreeze proteins, calcium binding, immunoglobulin-like domains, tandem repeats, protein crystal structure, protein rigidity, Antarctic bacteria, bacterial colonization, solution structure
- MeSH terms
- Antarctic Regions, Bacterial Proteins, Binding Sites, Calcium, Food, Ice, Immunoglobulins, Oxygen, Protein Binding, X-Ray Diffraction, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Marinomonas, Scattering, Small Angle
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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