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6evh
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Lipoaminopeptide helioferin A and B from Mycogone rosea== | |
| + | <StructureSection load='6evh' size='340' side='right' caption='[[6evh]], [[Resolution|resolution]] 0.90Å' scene=''> | ||
| + | == 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> | ||
| + | </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> | ||
| + | <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='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> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:29652258</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6evh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[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]] | ||
Revision as of 07:40, 18 July 2018
Lipoaminopeptide helioferin A and B from Mycogone rosea
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