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2m1f

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[[Image:2m1f.jpg|left|200px]]
 
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{{STRUCTURE_2m1f| PDB=2m1f | SCENE= }}
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==NMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicelles==
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<StructureSection load='2m1f' size='340' side='right'caption='[[2m1f]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Antiamoebin 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.
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===NMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicelles===
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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<ref>PMID:23681729</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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[[2m1f]] is a 1 chain structure with sequence from [http://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].
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<div class="pdbe-citations 2m1f" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Emericellopsis minima]]
[[Category: Emericellopsis minima]]
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[[Category: Gizatullina, A K.]]
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[[Category: Large Structures]]
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[[Category: Paramonov, A S.]]
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[[Category: Gizatullina AK]]
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[[Category: Shenkarev, Z O.]]
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[[Category: Paramonov AS]]
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[[Category: Antibiotic]]
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[[Category: Shenkarev ZO]]
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[[Category: Membrane-active]]
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[[Category: Peptaibol]]
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Current revision

NMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicelles

PDB ID 2m1f

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