2lr5
From Proteopedia
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| - | [[ | + | ==1H chemical shift assignments for micasin== |
| + | <StructureSection load='2lr5' size='340' side='right' caption='[[2lr5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2lr5]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LR5 OCA]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lr5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lr5 RCSB], [http://www.ebi.ac.uk/pdbsum/2lr5 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fungi are a newly emerging source of peptide antibiotics with therapeutic potential. Here, we report 17 new fungal defensin-like peptide (fDLP) genes and the detailed characterization of a corresponding synthetic fDLP (micasin) from a dermatophyte in terms of its structure, activity and therapeutic potential. NMR analysis showed that synthetic micasin adopts a "hallmark" cysteine-stablized alpha-helical and beta-sheet fold. It was active on both Gram-positive and Gram-negtive bacteria, and importantly it killed two clinical isolates of methicillin-resistant Staphylococcus aureus and the opportunistic pathogen Pseudomonas aeruginosa at low micromolar concentrations. Micasin killed approximately 100% of treated bacteria within 3 h through a membrane nondisruptive mechanism of action, and showed extremely low hemolysis and high serum stability. Consistent with these functional properties, micasin increases survival in mice infected by the pathogenic bacteria in a peritonitis model. Our work represents a valuable approach to explore novel peptide antibiotics from a large resource of fungal genomes. | ||
| - | + | Dermatophytic defensin with antiinfective potential.,Zhu S, Gao B, Harvey PJ, Craik DJ Proc Natl Acad Sci U S A. 2012 May 29;109(22):8495-500. Epub 2012 May 14. PMID:22586077<ref>PMID:22586077</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Craik, D J.]] | [[Category: Craik, D J.]] | ||
[[Category: Harvey, P J.]] | [[Category: Harvey, P J.]] | ||
[[Category: Zhu, S.]] | [[Category: Zhu, S.]] | ||
[[Category: Antimicrobial protein]] | [[Category: Antimicrobial protein]] | ||
Revision as of 08:43, 7 May 2014
1H chemical shift assignments for micasin
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