View source for 4k82


==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=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RANSP_LEPVA RANSP_LEPVA] Acts as a surfactant (PubMed:18689424, PubMed:24442854). 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 ==
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<ref>PMID:24442854</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4k82" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leptodactylus vastus]]
[[Category: Bezerra GA]]
[[Category: Gruber K]]
[[Category: Hissa DC]]
[[Category: Melo VMM]]