View source for 2wgo


==Structure of ranaspumin-2, a surfactant protein from the foam nests of a tropical frog==
<StructureSection load='2wgo' size='340' side='right'caption='[[2wgo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wgo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Engystomops_pustulosus Engystomops pustulosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WGO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 models</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=2wgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wgo OCA], [https://pdbe.org/2wgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wgo RCSB], [https://www.ebi.ac.uk/pdbsum/2wgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wgo ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Ranaspumin-2 (Rsn-2) is a monomeric, 11 kDa surfactant protein identified as one of the major foam nest components of the tungara frog (Engystomops pustulosus), with an amino acid sequence unlike any other protein described so far. We report here on its structure in solution as determined by high-resolution NMR analysis, together with investigations of its conformation and packing at the air-water interface using a combination of infrared and neutron reflectivity techniques. Despite the lack of any significant sequence similarity, Rsn-2 in solution adopts a compact globular fold characteristic of the cystatin family, comprising a single helix over a four-stranded sheet, in a motif not previously associated with surfactant activity. The NMR structure of Rsn-2 shows no obvious amphiphilicity that might be anticipated for a surfactant protein. This suggests that it must undergo a significant conformational change when incorporated into the air-water interface that may involve a hinge-bending, clamshell opening of the separate helix and sheet segments to expose hydrophobic faces to air while maintaining the highly polar surfaces in contact with the underlying water layer. This model is supported by direct observation of the relative orientations of secondary structure elements at the interface by infrared reflection absorption spectroscopy, and by protein packing densities determined from neutron reflectivity profiles.

Ranaspumin-2: structure and function of a surfactant protein from the foam nests of a tropical frog.,Mackenzie CD, Smith BO, Meister A, Blume A, Zhao X, Lu JR, Kennedy MW, Cooper A Biophys J. 2009 Jun 17;96(12):4984-92. PMID:19527658<ref>PMID:19527658</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Engystomops pustulosus]]
[[Category: Large Structures]]
[[Category: Cooper A]]
[[Category: Kennedy MW]]
[[Category: Mackenzie CD]]
[[Category: Smith BO]]