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[[Image:1aj1.gif|left|200px]]
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[[Image:1aj1.png|left|200px]]


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{{STRUCTURE_1aj1|  PDB=1aj1  |  SCENE=  }}  
{{STRUCTURE_1aj1|  PDB=1aj1  |  SCENE=  }}  


'''NMR STRUCTURE OF THE LANTIBIOTIC ACTAGARDINE, 15 STRUCTURES'''
===NMR STRUCTURE OF THE LANTIBIOTIC ACTAGARDINE, 15 STRUCTURES===




==Overview==
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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.
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{{ABSTRACT_PUBMED_9219543}}


==About this Structure==
==About this Structure==
1AJ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Actinoplanes_liguriae_and_actinoplanes_garbadinensis Actinoplanes liguriae and actinoplanes garbadinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJ1 OCA].  
1AJ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Actinoplanes_liguriae_and_actinoplanes_garbadinensis Actinoplanes liguriae and actinoplanes garbadinensis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJ1 OCA].  


==Reference==
==Reference==
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[[Category: Peptide antibiotic]]
[[Category: Peptide antibiotic]]
[[Category: Transglycosylase inhibitor]]
[[Category: Transglycosylase inhibitor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:19:59 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:57:12 2008''

Revision as of 13:57, 30 June 2008

File:1aj1.png

Template:STRUCTURE 1aj1

NMR STRUCTURE OF THE LANTIBIOTIC ACTAGARDINE, 15 STRUCTURES

Template:ABSTRACT PUBMED 9219543

About this Structure

1AJ1 is a Single protein structure of sequence from Actinoplanes liguriae and actinoplanes garbadinensis. Full experimental 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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