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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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <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 [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> | | <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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1joh|1joh]], [[1ob4|1ob4]], [[1ob6|1ob6]], [[1ob7|1ob7]], [[1dlz|1dlz]], [[1ih9|1ih9]], [[1r9u|1r9u]]</div></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></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=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> | | <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> |
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| | [[Category: Emericellopsis minima]] | | [[Category: Emericellopsis minima]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gizatullina, A K]] | + | [[Category: Gizatullina AK]] |
| - | [[Category: Paramonov, A S]] | + | [[Category: Paramonov AS]] |
| - | [[Category: Shenkarev, Z O]] | + | [[Category: Shenkarev ZO]] |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Membrane-active]]
| + | |
| - | [[Category: Peptaibol]]
| + | |
| Structural highlights
2m1f is a 1 chain structure with sequence from Emericellopsis minima. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | Solution NMR, 20 models |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
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.
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
- ↑ Shenkarev ZO, Paramonov AS, Lyukmanova EN, Gizatullina AK, Zhuravleva AV, Tagaev AA, Yakimenko ZA, Telezhinskaya IN, Kirpichnikov MP, Ovchinnikova TV, Arseniev AS. Peptaibol antiamoebin I: spatial structure, backbone dynamics, interaction with bicelles and lipid-protein nanodiscs, and pore formation in context of barrel-stave model. Chem Biodivers. 2013 May;10(5):838-63. doi: 10.1002/cbdv.201200421. PMID:23681729 doi:10.1002/cbdv.201200421
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