6gil
From Proteopedia
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==NMR structure of temporin B in SDS micelles== | ==NMR structure of temporin B in SDS micelles== | ||
| - | <StructureSection load='6gil' size='340' side='right' caption='[[6gil | + | <StructureSection load='6gil' size='340' side='right'caption='[[6gil]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6gil]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GIL OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6gil]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rana_temporaria Rana temporaria]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GIL FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6gil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gil OCA], [https://pdbe.org/6gil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gil RCSB], [https://www.ebi.ac.uk/pdbsum/6gil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gil ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TPB_RANTE TPB_RANTE] Amphipathic alpha-helical antimicrobial peptide with potent activity against Gram-positive bacteria, weak activity against Gram-negative bacteria, and moderate activity against fungi (PubMed:27351824, PubMed:30718667, PubMed:9022710). Mainly acts by causing membrane permeabilization, but is unable to forme pore-like openings (Probable). Is also able to penetrate eukaryotic cells (keratinocytes), and kill intracellular S.aureus (both wild-type and MRSA) without injuring host cells (PubMed:24514087). Shows inhibitory effect on biofilm formation of Gram-positive bacteria, but not of Gram-negative bacteria (PubMed:27351824, PubMed:28443279). Shows antiviral activity against herpes simplex virus 1 (HSV-1) by disrupting the viral envelope (PubMed:29483113). Also displays anti-leishmania activity by damaging parasite membrane (PubMed:15513914, PubMed:25668079). Does not show hemolytic activity (PubMed:15513914, PubMed:28443279, PubMed:9022710). Acts synergistically with temporin-L that improves temporin-1Tb activity by preventing its self-association in lipopolysaccharides (LPS) (PubMed:16867990, PubMed:21586570). In vitro, promotes cell migration and wound healing (PubMed:24514087).<ref>PMID:15513914</ref> <ref>PMID:16867990</ref> <ref>PMID:21586570</ref> <ref>PMID:24514087</ref> <ref>PMID:25668079</ref> <ref>PMID:27351824</ref> <ref>PMID:28443279</ref> <ref>PMID:29483113</ref> <ref>PMID:30718667</ref> <ref>PMID:9022710</ref> <ref>PMID:10691983</ref> <ref>PMID:11576327</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Antimicrobial peptides (AMPs) are a potential source of new molecules to counter the increase in antimicrobial resistant infections but a better understanding of their properties is required to understand their native function and for effective translation as therapeutics. Details of the mechanism of their interaction with the bacterial plasma membrane are desired since damage or penetration of this structure is considered essential for AMPs activity. Relatively modest modifications to AMPs primary sequence can induce substantial changes in potency and/or spectrum of activity but, hitherto, have not been predicted to substantially alter the mechanism of interaction with the bacterial plasma membrane. Here we use a combination of molecular dynamics simulations, circular dichroism, solid-state NMR and patch clamp to investigate the extent to which temporin B and its analogues can be distinguished both in vitro and in silico on the basis of their interactions with model membranes. Enhancing the hydrophobicity of the N-terminus and cationicity of the C-terminus in temporin B improves its membrane activity and potency against both Gram-negative and Gram-positive bacteria. In contrast, enhancing the cationicity of the N-terminus abrogates its ability to trigger channel conductance and renders it ineffective against Gram-positive bacteria while nevertheless enhancing its potency against Escherichia coli. Our findings suggest even closely related AMPs may target the same bacterium with fundamentally differing mechanisms of action. | ||
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| + | Minor sequence modifications in temporin B cause drastic changes in antibacterial potency and selectivity by fundamentally altering membrane activity.,Manzo G, Ferguson PM, Gustilo VB, Hind CK, Clifford M, Bui TT, Drake AF, Atkinson RA, Sutton JM, Batoni G, Lorenz CD, Phoenix DA, Mason AJ Sci Rep. 2019 Feb 4;9(1):1385. doi: 10.1038/s41598-018-37630-3. PMID:30718667<ref>PMID:30718667</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6gil" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Rana temporaria]] |
| - | [[Category: | + | [[Category: Manzo G]] |
| - | [[Category: | + | [[Category: Mason JA]] |
| - | + | ||
Current revision
NMR structure of temporin B in SDS micelles
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