1ut3

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(Difference between revisions)

Revision as of 14:43, 10 September 2015

SOLUTION STRUCTURE OF SPHENISCIN-2, A BETA-DEFENSIN FROM PENGUIN STOMACH PRESERVING FOOD

Structural highlights

1ut3 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[SPHE2_APTPA] Has antifungal activity and antibacterial activity against Gram-positive and Gram-negative bacteria. Involved in the process of food preservation in the stomach during the incubation fast. May also be present during infection.^[1]

Publication Abstract from PubMed

Recently two beta-defensins, named spheniscins, have been isolated from the stomach content of the king penguin (Aptenodytes patagonicus), which is capable of preserving food for several weeks during egg incubation (Thouzeau, C., Le Maho, Y., Froget, G., Sabatier, L., Le Bohec, C., Hoffmann, J. A., and Bulet, P. (2003) J. Biol. Chem. 278, 51053-51058). It has been proposed that, in combination with other antimicrobial peptides, spheniscins may be involved in this long term preservation of food in the bird's stomach. To draw some structure/function features, the three-dimensional structure in aqueous solution of the most abundant spheniscin (Sphe-2) was determined by two-dimensional NMR and molecular modeling techniques. The overall fold of Sphe-2 includes a three-stranded antiparallel beta-sheet stabilized by three disulfide bridges with a pairing typical of beta-defensins. In addition, the N-terminal segment shows helical features on most structures. Sphe-2 is highly cationic, and its surface displays a hydrophobic patch. Comparative modeling revealed that this patch is preserved in avian defensins. The activity of Sphe-2 against a pathogenic Gram-positive strain was retained in vitro in the conditions of osmolarity found in penguin stomach content and also in different salt concentrations and compositions up to those reported for seawater. Comparison with structurally related mammalian beta-defensins showed that the hydrophobic patch is not preserved in mammalian beta-defensins and that the high cationicity of Sphe-2 is presumably the critical factor for its retained activity in high salt concentrations. Such peculiarities, in addition to a broad activity spectrum, suggest that penguin defensins may represent interesting probes for the design of highly efficient antibiotics to fight off pathogens that develop in relatively salt-rich body fluids.

Solution structure of spheniscin, a beta-defensin from the penguin stomach.,Landon C, Thouzeau C, Labbe H, Bulet P, Vovelle F J Biol Chem. 2004 Jul 16;279(29):30433-9. Epub 2004 Apr 30. PMID:15123713^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Thouzeau C, Le Maho Y, Froget G, Sabatier L, Le Bohec C, Hoffmann JA, Bulet P. Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus. J Biol Chem. 2003 Dec 19;278(51):51053-8. Epub 2003 Oct 2. PMID:14525994 doi:10.1074/jbc.M306839200
↑ Landon C, Thouzeau C, Labbe H, Bulet P, Vovelle F. Solution structure of spheniscin, a beta-defensin from the penguin stomach. J Biol Chem. 2004 Jul 16;279(29):30433-9. Epub 2004 Apr 30. PMID:15123713 doi:10.1074/jbc.M401338200

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/1ut3"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1ut3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UT3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UT3 FirstGlance]. <br>
-</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=1ut3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ut3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ut3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ut3 PDBsum]</span></td></tr>
+</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=1ut3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ut3 OCA], [http://pdbe.org/1ut3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ut3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ut3 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SPHE2_APTPA SPHE2_APTPA]] Has antifungal activity and antibacterial activity against Gram-positive and Gram-negative bacteria. Involved in the process of food preservation in the stomach during the incubation fast. May also be present during infection.<ref>PMID:14525994</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 13: / Line 15: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ut3" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1ut3

From Proteopedia

Revision as of 14:43, 10 September 2015

SOLUTION STRUCTURE OF SPHENISCIN-2, A BETA-DEFENSIN FROM PENGUIN STOMACH PRESERVING FOOD

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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