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==Nmr structure of hen egg beta-defensin gallin (chicken ovo-defensin)==
<StructureSection load='2mjk' size='340' side='right'caption='[[2mjk]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mjk]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MJK FirstGlance]. <br>
</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=2mjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjk OCA], [https://pdbe.org/2mjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mjk RCSB], [https://www.ebi.ac.uk/pdbsum/2mjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mjk ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Gallin is a 41-residue protein, first identified as a minor component of hen egg white, and found to be antimicrobial against Escherichia coli. Gallin may participate in the protection of the embryo during its development in the egg. Its sequence is related to antimicrobial beta-defensin peptides. In the present study, gallin was chemically synthesized 1) to further investigate its antimicrobial spectrum, and 2) to solve its 3D NMR structure, and thus gain insight into structure-function relationships, a prerequisite to understand its mode(s) of action. Antibacterial assays confirmed that gallin was active against Escherichia coli, but no additional antibacterial activity was observed against the other Gram-positive or Gram-negative bacteria tested. The 3D structure of gallin, which is the first ovo-defensin structure to have been solved to date, displays a new five-stranded arrangement. The gallin 3D fold contains the three-stranded antiparallel beta-sheet and the disulfide bridge array typical of vertebrate beta-defensins. Gallin can therefore be unambiguously classified as a beta-defensin. However, an additional short two-stranded beta-sheet reveals that gallin, and presumably the other ovo-defensins, form a new structural sub-family of beta-defensins. Moreover, gallin and the other ovo-defensins calculated by homology modelling exhibit atypical hydrophobic surface properties, compared with the already known vertebrate beta-defensins. These specific structural features of gallin might be related to its restricted activity against E. coli, and/or to other yet unknown functions. This work provides initial understanding of a critical sequence-structure-function relationship for the ovo-defensin family.

3D NMR structure of hen egg gallin (chicken ovo-defensin) reveals a new variation of the beta-defensin fold.,Herve V, Meudal H, Labas V, Rehault Godbert S, Gautron J, Berges M, Guyot N, Delmas AF, Nys Y, Landon C J Biol Chem. 2014 Jan 17. PMID:24443564<ref>PMID:24443564</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: Large Structures]]
[[Category: Landon, C]]
[[Category: Meudal, H]]
[[Category: Antimicrobial protein]]