2k35

From Proteopedia

(Difference between revisions)

Current revision

Hydramacin-1: Structure and antibacterial activity of a peptide from the basal metazoan Hydra

Structural highlights

2k35 is a 1 chain structure with sequence from Hydra. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 25 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HYDMA_HYDVU Cationic antimicrobial peptide potently active against Gram-positive and Gram-negative bacteria including multi-resistant human pathogenic strains. Is not active against the Gram-positive Coccus species, Gram-negative non-fermentation species and against the fungus C.albicans. It leads to aggregation of bacteria as an initial step of its bactericidal mechanism. Aggregated cells are connected via electron-dense contacts and adopt a thorn apple-like morphology. Hydramycin contains a belt of positively charged residues that separate two hydrophobic areas. This structure may explain the observed aggregation of bacteria, since each of these areas can immerse into the outer leaflets of the membranes of two individual bacteria. Is able to permeabilize membranes of viable bacteria at low and neutral pH values, but no pore-forming activity is not detected.^[1] ^[2]

Publication Abstract from PubMed

Hydramacin-1 is a novel antimicrobial protein recently discovered during investigations of the epithelial defense of the ancient metazoan Hydra. The amino acid sequence of hydramacin-1 shows no sequence homology to any known antimicrobial proteins. Determination of the solution structure revealed that hydramacin-1 possesses a disulfide bridge-stabilized alphabeta motif. This motif is the common scaffold of the knottin protein fold. The structurally closest relatives are the scorpion oxin-like superfamily. Within this superfamily hydramacin-1 establishes a new family of proteins that all share antimicrobial activity. Hydramacin-1 is potently active against Gram-positive and Gram-negative bacteria including multi-resistant human pathogenic strains. It leads to aggregation of bacteria as an initial step of its bactericidal mechanism. Aggregated cells are connected via electron-dense contacts and adopt a thorn apple-like morphology. Analysis of the hydramacin-1 structure revealed an unusual distribution of amino acid side chains on the surface. A belt of positively charged residues is sandwiched by two hydrophobic areas. Based on this characteristic surface feature and on biophysical analysis of protein-membrane interactions, we propose a model that describes the aggregation effect exhibited by hydramacin-1.

Hydramacin-1, structure and antibacterial activity of a protein from the basal metazoan Hydra.,Jung S, Dingley AJ, Augustin R, Anton-Erxleben F, Stanisak M, Gelhaus C, Gutsmann T, Hammer MU, Podschun R, Bonvin AM, Leippe M, Bosch TC, Grotzinger J J Biol Chem. 2009 Jan 16;284(3):1896-905. Epub 2008 Nov 19. PMID:19019828^[3]

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

References

↑ Bosch TC, Augustin R, Anton-Erxleben F, Fraune S, Hemmrich G, Zill H, Rosenstiel P, Jacobs G, Schreiber S, Leippe M, Stanisak M, Grötzinger J, Jung S, Podschun R, Bartels J, Harder J, Schröder JM. Uncovering the evolutionary history of innate immunity: the simple metazoan Hydra uses epithelial cells for host defence. Dev Comp Immunol. 2009 Apr;33(4):559-69. PMID:19013190 doi:10.1016/j.dci.2008.10.004
↑ Jung S, Dingley AJ, Augustin R, Anton-Erxleben F, Stanisak M, Gelhaus C, Gutsmann T, Hammer MU, Podschun R, Bonvin AM, Leippe M, Bosch TC, Grotzinger J. Hydramacin-1, structure and antibacterial activity of a protein from the basal metazoan Hydra. J Biol Chem. 2009 Jan 16;284(3):1896-905. Epub 2008 Nov 19. PMID:19019828 doi:10.1074/jbc.M804713200
↑ Jung S, Dingley AJ, Augustin R, Anton-Erxleben F, Stanisak M, Gelhaus C, Gutsmann T, Hammer MU, Podschun R, Bonvin AM, Leippe M, Bosch TC, Grotzinger J. Hydramacin-1, structure and antibacterial activity of a protein from the basal metazoan Hydra. J Biol Chem. 2009 Jan 16;284(3):1896-905. Epub 2008 Nov 19. PMID:19019828 doi:10.1074/jbc.M804713200

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/2k35"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2k35]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydra Hydra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K35 FirstGlance]. <br>
-</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+</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=2k35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k35 OCA], [https://pdbe.org/2k35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k35 RCSB], [https://www.ebi.ac.uk/pdbsum/2k35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k35 ProSAT]</span></td></tr>
 </table>

2k35

From Proteopedia

Current revision

Hydramacin-1: Structure and antibacterial activity of a peptide from the basal metazoan Hydra

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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