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Cavalcante Hissa, D; Arruda Bezerra, G; Birner-Gruenberger, R; Paulino Silva, L; Usón, I; Gruber, K; Maciel Melo, VM.
Unique crystal structure of a novel surfactant protein from the foam nest of the frog Leptodactylus vastus.
Chembiochem. 2014; 15(3):393-398
Doi: 10.1002/cbic.201300726
Web of Science
PubMed
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- Co-Autor*innen der Med Uni Graz
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Birner-Grünberger Ruth
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- Abstract:
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Breeding by releasing eggs into stable biofoams ("foam nests") is a peculiar reproduction mode within anurans, fish, and tunicates; not much is known regarding the biochemistry or molecular mechanisms involved. Lv-ranaspumin (Lv-RSN-1) is the predominant protein from the foam nest of the frog Leptodactylus vastus. This protein shows natural surfactant activity, which is assumed to be crucial for stabilizing foam nests. We elucidated the amino acid sequence of Lv-RSN-1 by de novo sequencing with mass-spectrometry and determined the high-resolution X-ray structure of the protein. It has a unique fold mainly composed of a bundle of 11 α-helices and two small antiparallel β-strands. Lv-RSN-1 has a surface rich in hydrophilic residues and a lipophilic cavity in the region of the antiparallel β-sheet. It possesses intrinsic surface-active properties, reducing the surface tension of water from 73 to 61 mN m(-1) (15 μg mL(-1)). Lv-RSN-1 belongs to a new class of surfactants proteins for which little has been reported regarding structure or function.
Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
- Find related publications in this database (using NLM MeSH Indexing)
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Animals -
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Anura - metabolism
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Circular Dichroism -
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Crystallography, X-Ray -
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Databases, Protein -
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Hydrophobic and Hydrophilic Interactions -
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Mass Spectrometry -
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Protein Structure, Secondary -
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Protein Structure, Tertiary -
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Proteins - chemistry
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Proteins - metabolism
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Sequence Analysis, Protein -
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Surface Tension -
- Find related publications in this database (Keywords)
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amphibians
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Lv-ranaspumin
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mass spectrometry
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structural biology
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surfactants