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2k35
From Proteopedia
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| - | [[ | + | ==Hydramacin-1: Structure and antibacterial activity of a peptide from the basal metazoan Hydra== |
| + | <StructureSection load='2k35' size='340' side='right' caption='[[2k35]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2k35]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K35 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=2k35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k35 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k35 RCSB], [http://www.ebi.ac.uk/pdbsum/2k35 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:19019828</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Hydra]] | [[Category: Hydra]] | ||
[[Category: Bosch, T.]] | [[Category: Bosch, T.]] | ||
Revision as of 15:27, 12 October 2014
Hydramacin-1: Structure and antibacterial activity of a peptide from the basal metazoan Hydra
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