| http://purl.uniprot.org/citations/9219543 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9219543 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9219543 | http://www.w3.org/2000/01/rdf-schema#comment | "The three-dimensional solution structure of the lantibiotic actagardine was determined at high resolution by homonuclear and heteronuclear two-dimensional and three-dimensional NMR spectroscopy in [2H3]acetonitrile/H2O (7:3). 133 non-trivial distance and 22 torsional-angle constraints were derived from the NMR data. An ensemble of 15 low-energy structures was calculated by distance geometry followed by an iterative relaxation-matrix-refinement procedure. The rmsd of the backbone coordinates with respect to the average structure was 17 pm. The two distinct thioether ring systems 1-6 and 7-19 were even better defined, with backbone rmsd of 10 pm and 14 pm, respectively. Actagardine shows a rigid compact globular shape based on the constraining bridging pattern, which is composed of an N-terminal lanthionine ring from residues 1-6 and three intertwined C-terminal methyllanthionine rings comprising residues 7-12, 9-17 and 14-19. In addition, this C-terminal ring system is stabilised by a short antiparallel beta sheet. A feature of the actagardine structure is the presence of two putative binding pockets. A pocket is generated by the covalent constraints of the C-terminal thioether ring system. The rim of this pocket is built up by a loop structure comprising residues 12-19, whose backbone amide protons are all directed to the centre of the pocket. The second pocket is formed by an L-shaped orientation of the N-terminal and C-terminal thioether ring systems. The only two hydrophilic amino acid residues of actagardine, Glu11 and Ser2, are directed to this pocket. A region of high sequence similarity with the related lantibiotic mersacidin is located exactly at the position of the second pocket (residues 3-12). This suggests that the second pocket is responsible for the antibiotic mode of action of actagardine and mersacidin as inhibitors of the murein biosynthesis of gram-positive bacteria."xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1997.00809.x"xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1997.00809.x"xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/author | "Jung G."xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/author | "Jung G."xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/author | "Zimmermann N."xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/author | "Zimmermann N."xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/pages | "809-819"xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/pages | "809-819"xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/title | "The three-dimensional solution structure of the lantibiotic murein-biosynthesis-inhibitor actagardine determined by NMR."xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/title | "The three-dimensional solution structure of the lantibiotic murein-biosynthesis-inhibitor actagardine determined by NMR."xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/volume | "246"xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://purl.uniprot.org/core/volume | "246"xsd:string |
| http://purl.uniprot.org/citations/9219543 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9219543 |
| http://purl.uniprot.org/citations/9219543 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9219543 |
| http://purl.uniprot.org/citations/9219543 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9219543 |
| http://purl.uniprot.org/citations/9219543 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9219543 |
| http://purl.uniprot.org/uniprot/P56650 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9219543 |
| http://purl.uniprot.org/uniprot/P56650#attribution-1361BDF202D9E68A9287C07414D2DEE9 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/9219543 |