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| <StructureSection load='5mas' size='340' side='right'caption='[[5mas]], [[Resolution|resolution]] 0.84Å' scene=''> | | <StructureSection load='5mas' size='340' side='right'caption='[[5mas]], [[Resolution|resolution]] 0.84Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5mas]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Emericellopsis_donezkii Emericellopsis donezkii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MAS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Emericellopsis_donezkii Emericellopsis donezkii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MAS 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">X-ray diffraction, [[Resolution|Resolution]] 0.84Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g13|4g13]], [[4g14|4g14]]</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'>[http://proteopedia.org/fgij/fg.htm?mol=5mas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mas OCA], [http://pdbe.org/5mas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mas RCSB], [http://www.ebi.ac.uk/pdbsum/5mas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mas 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=5mas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mas OCA], [https://pdbe.org/5mas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mas RCSB], [https://www.ebi.ac.uk/pdbsum/5mas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mas ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/A0A1U7Q1Y9_9HYPO A0A1U7Q1Y9_9HYPO] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| [[Category: Emericellopsis donezkii]] | | [[Category: Emericellopsis donezkii]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Gessmann, R]] | + | [[Category: Gessmann R]] |
- | [[Category: Petratos, K]] | + | [[Category: Petratos K]] |
- | [[Category: Alpha-helix]]
| + | |
- | [[Category: Antibiotic]]
| + | |
- | [[Category: Antibiotic peptide]]
| + | |
- | [[Category: Peptaibol]]
| + | |
| Structural highlights
5mas is a 1 chain structure with sequence from Emericellopsis donezkii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Method: | X-ray diffraction, Resolution 0.84Å |
Ligands: | , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A0A1U7Q1Y9_9HYPO
Publication Abstract from PubMed
Bergofungin is a peptide antibiotic that is produced by the ascomycetous fungus Emericellopsis donezkii HKI 0059 and belongs to peptaibol subfamily 2. The crystal structure of bergofungin A has been determined and refined to 0.84 A resolution. This is the second crystal structure of a natural 15-residue peptaibol, after that of samarosporin I. The amino-terminal phenylalanine residue in samarosporin I is exchanged to a valine residue in bergofungin A. According to agar diffusion tests, this results in a nearly inactive antibiotic peptide compared with the moderately active samarosporin I. Crystals were obtained from methanol solutions of purified bergofungin mixed with water. Although there are differences in the intramolecular hydrogen-bonding scheme of samarosporin I, the overall folding is very similar for both peptaibols, namely 310-helical at the termini and alpha-helical in the middle of the molecules. Bergofungin A and samarosporin I molecules are arranged in a similar way in both lattices. However, the packing of bergofungin A exhibits a second solvent channel along the twofold axis. This latter channel occurs in the vicinity of the N-terminus, where the natural substitution resides.
A natural, single-residue substitution yields a less active peptaibiotic: the structure of bergofungin A at atomic resolution.,Gessmann R, Axford D, Bruckner H, Berg A, Petratos K Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):95-100. doi:, 10.1107/S2053230X17001236. Epub 2017 Jan 27. PMID:28177320[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gessmann R, Axford D, Bruckner H, Berg A, Petratos K. A natural, single-residue substitution yields a less active peptaibiotic: the structure of bergofungin A at atomic resolution. Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):95-100. doi:, 10.1107/S2053230X17001236. Epub 2017 Jan 27. PMID:28177320 doi:http://dx.doi.org/10.1107/S2053230X17001236
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