2lr5: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 2lr5 is ~~ON HOLD~~

==1H chemical shift assignments for micasin==

== Structural highlights ==

<table><tr><td colspan='2'>[[2lr5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Microsporum_canis Microsporum canis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LR5 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=2lr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lr5 OCA], [https://pdbe.org/2lr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lr5 RCSB], [https://www.ebi.ac.uk/pdbsum/2lr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lr5 ProSAT]</span></td></tr>

</table>

== 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.

~~Authors: harvey~~, ~~p.j.~~, ~~craik~~, d.j.~~, zhu, s~~.

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>

~~Description~~: ~~1H chemical shift assignments for micasin~~

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

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Microsporum canis]]

[[Category: Craik DJ]]

[[Category: Harvey PJ]]

[[Category: Zhu S]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2lr5 is ON HOLD
+==1H chemical shift assignments for micasin==
+<StructureSection load='2lr5' size='340' side='right'caption='[[2lr5]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2lr5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Microsporum_canis Microsporum canis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LR5 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=2lr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lr5 OCA], [https://pdbe.org/2lr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lr5 RCSB], [https://www.ebi.ac.uk/pdbsum/2lr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lr5 ProSAT]</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.
-Authors: harvey, p.j., craik, d.j., zhu, s.
+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>
-Description: 1H chemical shift assignments for micasin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2lr5" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Microsporum canis]]
+[[Category: Craik DJ]]
+[[Category: Harvey PJ]]
+[[Category: Zhu S]]