4k83 | pdb_00004k83
Crystal structure of lv-ranaspumin (Lv-RSN-1) from the foam nest of Leptodactylus vastus, orthorhombic crystal form
Structural highlights
FunctionRANSP_LEPVA Acts as a surfactant (PubMed:24442854, PubMed:18689424). Is the major protein constituent (45%) of foam nests (PubMed:27460953). Has no antimicrobial activity, no larvicidal activity, and is not toxic to mice (PubMed:18689424).[1] [2] [3] Publication Abstract from PubMedBreeding 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 alpha-helices and two small antiparallel beta-strands. Lv-RSN-1 has a surface rich in hydrophilic residues and a lipophilic cavity in the region of the antiparallel beta-sheet. It possesses intrinsic surface-active properties, reducing the surface tension of water from 73 to 61 mN m(-1) (15 mug mL(-1)). Lv-RSN-1 belongs to a new class of surfactants proteins for which little has been reported regarding structure or function. Unique crystal structure of a novel surfactant protein from the foam nest of the frog Leptodactylus vastus.,Cavalcante Hissa D, Arruda Bezerra G, Birner-Gruenberger R, Paulino Silva L, Uson I, Gruber K, Maciel Melo VM Chembiochem. 2014 Feb 10;15(3):393-8. doi: 10.1002/cbic.201300726. Epub 2014 Jan , 17. PMID:24442854[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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