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4k82

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Crystal structure of lv-ranaspumin (Lv-RSN-1) from the foam nest of Leptodactylus vastus, monoclinic crystal form

Structural highlights

4k82 is a 1 chain structure with sequence from Leptodactylus vastus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RANSP_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 PubMed

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 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

↑ Hissa DC, Vasconcelos IM, Carvalho AF, Nogueira VL, Cascon P, Antunes AS, de Macedo GR, Melo VM. Novel surfactant proteins are involved in the structure and stability of foam nests from the frog Leptodactylus vastus. J Exp Biol. 2008 Aug;211(Pt 16):2707-11. doi: 10.1242/jeb.019315. PMID:18689424 doi:http://dx.doi.org/10.1242/jeb.019315
↑ Cavalcante Hissa D, Arruda Bezerra G, Birner-Gruenberger R, Paulino Silva L, Uson 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 Feb 10;15(3):393-8. doi: 10.1002/cbic.201300726. Epub 2014 Jan , 17. PMID:24442854 doi:http://dx.doi.org/10.1002/cbic.201300726
↑ Hissa DC, Bezerra WM, Freitas CD, Ramos MV, Lopes JL, Beltramini LM, Roberto IJ, Cascon P, Melo VM. Frog Foam Nest Protein Diversity and Synthesis. J Exp Zool A Ecol Genet Physiol. 2016 Aug;325(7):425-33. doi: 10.1002/jez.2027. , Epub 2016 Jul 27. PMID:27460953 doi:http://dx.doi.org/10.1002/jez.2027
↑ Cavalcante Hissa D, Arruda Bezerra G, Birner-Gruenberger R, Paulino Silva L, Uson 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 Feb 10;15(3):393-8. doi: 10.1002/cbic.201300726. Epub 2014 Jan , 17. PMID:24442854 doi:http://dx.doi.org/10.1002/cbic.201300726

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4k82"

@@ Line 1: / Line 1: @@
 ==Crystal structure of lv-ranaspumin (Lv-RSN-1) from the foam nest of Leptodactylus vastus, monoclinic crystal form==
-<StructureSection load='4k82' size='340' side='right' caption='[[4k82]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='4k82' size='340' side='right'caption='[[4k82]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4k82]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leptodactylus_vastus Leptodactylus vastus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K82 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4k82]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptodactylus_vastus Leptodactylus vastus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K82 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k83|4k83]]</td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k82 OCA], [https://pdbe.org/4k82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k82 RCSB], [https://www.ebi.ac.uk/pdbsum/4k82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k82 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k82 OCA], [http://pdbe.org/4k82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k82 RCSB], [http://www.ebi.ac.uk/pdbsum/4k82 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k82 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/RANSP_LEPVA RANSP_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).<ref>PMID:18689424</ref> <ref>PMID:24442854</ref> <ref>PMID:27460953</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 21: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Leptodactylus vastus]]
-[[Category: Bezerra, G A]]
+[[Category: Bezerra GA]]
-[[Category: Gruber, K]]
+[[Category: Gruber K]]
-[[Category: Hissa, D C]]
+[[Category: Hissa DC]]
-[[Category: Melo, V M.M]]
+[[Category: Melo VMM]]
-[[Category: Alpha-helical]]
-[[Category: Amphibian]]
-[[Category: Foam nest]]
-[[Category: Frog]]
-[[Category: Structural protein]]
-[[Category: Surfactant protein]]

4k82

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Current revision

Crystal structure of lv-ranaspumin (Lv-RSN-1) from the foam nest of Leptodactylus vastus, monoclinic crystal form

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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