2lr5: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2lr5.jpg|left|200px]]
==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.


{{STRUCTURE_2lr5|  PDB=2lr5  |  SCENE=  }}
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>


===1H chemical shift assignments for micasin===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_22586077}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2lr5]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LR5 OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:022586077</ref><references group="xtra"/>
[[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]]
Retrieved from "https://proteopedia.org/2lr5"