1aj1
From Proteopedia
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|PDB= 1aj1 |SIZE=350|CAPTION= <scene name='initialview01'>1aj1</scene> | |PDB= 1aj1 |SIZE=350|CAPTION= <scene name='initialview01'>1aj1</scene> | ||
|SITE= <scene name='pdbsite=MER:Homology+Region+To+Mersacidin'>MER</scene> | |SITE= <scene name='pdbsite=MER:Homology+Region+To+Mersacidin'>MER</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aj1 OCA], [http://www.ebi.ac.uk/pdbsum/1aj1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aj1 RCSB]</span> | ||
}} | }} | ||
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[[Category: transglycosylase inhibitor]] | [[Category: transglycosylase inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:41:17 2008'' |
Revision as of 15:41, 30 March 2008
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF THE LANTIBIOTIC ACTAGARDINE, 15 STRUCTURES
Overview
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.
About this Structure
1AJ1 is a Single protein structure of sequence from Actinoplanes liguriae and actinoplanes garbadinensis. Full crystallographic information is available from OCA.
Reference
The three-dimensional solution structure of the lantibiotic murein-biosynthesis-inhibitor actagardine determined by NMR., Zimmermann N, Jung G, Eur J Biochem. 1997 Jun 15;246(3):809-19. PMID:9219543
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