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| | ==Lipoaminopeptide helioferin A and B from Mycogone rosea== | | ==Lipoaminopeptide helioferin A and B from Mycogone rosea== |
| - | <StructureSection load='6evh' size='340' side='right' caption='[[6evh]], [[Resolution|resolution]] 0.90Å' scene=''> | + | <StructureSection load='6evh' size='340' side='right'caption='[[6evh]], [[Resolution|resolution]] 0.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6evh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycogone_rosea Mycogone rosea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EVH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6evh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycogone_rosea Mycogone rosea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EVH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F:FLUORIDE+ION'>F</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=BZK:'>BZK</scene>, <scene name='pdbligand=C9K:'>C9K</scene>, <scene name='pdbligand=C9N:'>C9N</scene>, <scene name='pdbligand=C9T:'>C9T</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=BZK:(2S,+4S,+6S)-2-amino-6-hydroxy-4-methyl-8-oxodecanoic+acid'>BZK</scene>, <scene name='pdbligand=C9K:2-[[(2~{S})-2-azanylpropyl]amino]ethanol'>C9K</scene>, <scene name='pdbligand=C9N:2-[[(2~{S})-2-azanylpropyl]-methyl-amino]ethanol'>C9N</scene>, <scene name='pdbligand=C9T:(2~{R})-2-methyloctanoic+acid'>C9T</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F:FLUORIDE+ION'>F</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6evh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6evh OCA], [http://pdbe.org/6evh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6evh RCSB], [http://www.ebi.ac.uk/pdbsum/6evh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6evh 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=6evh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6evh OCA], [https://pdbe.org/6evh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6evh RCSB], [https://www.ebi.ac.uk/pdbsum/6evh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6evh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mycogone rosea]] | | [[Category: Mycogone rosea]] |
| - | [[Category: Gessmann, R]] | + | [[Category: Gessmann R]] |
| - | [[Category: Petratos, K]] | + | [[Category: Petratos K]] |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Lipoaminopeptide]]
| + | |
| - | [[Category: Peptaibiotic]]
| + | |
| - | [[Category: Peptaibol]]
| + | |
| - | [[Category: Protonophoric]]
| + | |
| Structural highlights
6evh is a 1 chain structure with sequence from Mycogone rosea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 0.9Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
The crystal structure of the natural nonapeptide antibiotic helioferin has been determined and refined to 0.9 A resolution. Helioferin consists of helioferin A and B, which contain 2-(2'-aminopropyl)aminoethanol (Apae) and 2-[(2'-aminopropyl)methylamino]ethanol (Amae) at their respective alkanolamine termini. In addition, helioferin contains the unusual amino-acid residues alpha-aminoisobutyric acid (Aib) and (2S,4S,6S)-2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (Ahmod). The amino-terminus is capped with 2-methyl-n-1-octanoic acid (M8a). The peptide crystallizes with a 1:1 molar ratio of helioferin A and B in the monoclinic space group C2, with unit-cell parameters a = 34.711, b = 10.886, c = 17.150 A, beta = 93.05 degrees . The peptide backbone folds in a regular right-handed alpha-helical conformation, with eight intramolecular hydrogen bonds, all but one forming 5-->1 interactions. The two aliphatic chains of the fatty-acyl (M8a) and the second residue (Ahmod) extend out of the alpha-helical structure in opposite directions and lead to a corkscrew-like shape of the peptide molecule. Halogen anions (Cl(-) and F(-)) have been co-crystallized with the peptide molecules, implying a positive charge at the aminoalcohol end of the peptide. In the tightly packed crystal the helices are linked head to tail via the anions by electrostatic, hydrogen-bond and van der Waals interactions, forming continuous helical rods. Two nonparallel rods (forming an angle of 118 degrees ) interact directly via hydrogen bonds and via the anions, forming a double layer. Successive double layers are held together only via van der Waals contacts. The helical axes of successive double layers are also related by an angle of 118 degrees . The structure of helioferin reported here and the previously determined structure of the homologous leucinostatin A have a total straight length of about 21 A, indicating a different membrane-modifying bioactivity from that of long-chain, amphiphilic peptaibols.
The crystal structure of the lipoaminopeptaibol helioferin, an antibiotic peptide from Mycogone rosea.,Gessmann R, Bruckner H, Berg A, Petratos K Acta Crystallogr D Struct Biol. 2018 Apr 1;74(Pt 4):315-320. doi:, 10.1107/S2059798318001857. Epub 2018 Apr 3. PMID:29652258[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gessmann R, Bruckner H, Berg A, Petratos K. The crystal structure of the lipoaminopeptaibol helioferin, an antibiotic peptide from Mycogone rosea. Acta Crystallogr D Struct Biol. 2018 Apr 1;74(Pt 4):315-320. doi:, 10.1107/S2059798318001857. Epub 2018 Apr 3. PMID:29652258 doi:http://dx.doi.org/10.1107/S2059798318001857
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