2m1f: Difference between revisions
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==NMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicelles== | ==NMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicelles== | ||
<StructureSection load='2m1f' size='340' side='right' caption='[[2m1f | <StructureSection load='2m1f' size='340' side='right'caption='[[2m1f]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2m1f]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2m1f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Emericellopsis_minima Emericellopsis minima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M1F FirstGlance]. <br> | ||
</td></tr><tr id=' | </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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=DIV:D-ISOVALINE'>DIV</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=PHL:L-PHENYLALANINOL'>PHL</scene>, <scene name='pdbligand=PRD_000161:Antiamoebin+1'>PRD_000161</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m1f OCA], [https://pdbe.org/2m1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m1f RCSB], [https://www.ebi.ac.uk/pdbsum/2m1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m1f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Emericellopsis minima]] | [[Category: Emericellopsis minima]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Gizatullina AK]] | ||
[[Category: | [[Category: Paramonov AS]] | ||
[[Category: | [[Category: Shenkarev ZO]] | ||
Latest revision as of 14:51, 22 November 2023
NMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicellesNMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicelles
Structural highlights
Publication Abstract from PubMedAntiamoebin I (Aam-I) is a membrane-active peptaibol antibiotic isolated from fungal species belonging to the genera Cephalosporium, Emericellopsis, Gliocladium, and Stilbella. In comparison with other 16-amino acid-residue peptaibols, e.g., zervamicin IIB (Zrv-IIB), Aam-I possesses relatively weak biological and channel-forming activities. In MeOH solution, Aam-I demonstrates fast cooperative transitions between right-handed and left-handed helical conformation of the N-terminal (1-8) region. We studied Aam-I spatial structure and backbone dynamics in the membrane-mimicking environment (DMPC/DHPC bicelles)(1) ) by heteronuclear (1) H,(13) C,(15) N-NMR spectroscopy. Interaction with the bicelles stabilizes the Aam-I right-handed helical conformation retaining significant intramolecular mobility on the ms-mus time scale. Extensive ms-mus dynamics were also detected in the DPC and DHPC micelles and DOPG nanodiscs. In contrast, Zrv-IIB in the DPC micelles demonstrates appreciably lesser mobility on the mus-ms time scale. Titration with Mn(2+) and 16-doxylstearate paramagnetic probes revealed Aam-I binding to the bicelle surface with the N-terminus slightly immersed into hydrocarbon region. Fluctuations of the Aam-I helix between surface-bound and transmembrane (TM) state were observed in the nanodisc membranes formed from the short-chain (diC12 : 0) DLPC/DLPG lipids. All the obtained experimental data are in agreement with the barrel-stave model of TM pore formation, similarly to the mechanism proposed for Zrv-IIB and other peptaibols. The observed extensive intramolecular dynamics explains the relatively low activity of Aam-I. Peptaibol antiamoebin I: spatial structure, backbone dynamics, interaction with bicelles and lipid-protein nanodiscs, and pore formation in context of barrel-stave model.,Shenkarev ZO, Paramonov AS, Lyukmanova EN, Gizatullina AK, Zhuravleva AV, Tagaev AA, Yakimenko ZA, Telezhinskaya IN, Kirpichnikov MP, Ovchinnikova TV, Arseniev AS Chem Biodivers. 2013 May;10(5):838-63. doi: 10.1002/cbdv.201200421. PMID:23681729[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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