2IH0

NMR structure determination of a synthetic analogue of the iturinic antibiotic bacillomycin Lc

Summary for 2IH0

• Entry DOI: 10.2210/pdb2ih0/pdb
• Related: 2IGZ
• Related PRD ID: PRD_000720
• Descriptor: BACILLOMYCIN L-3 (1 entity in total)
• Functional Keywords: iturins, antifungal, cyclopeptide, lipopeptide, surfactant bacillomycin, antibiotic
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 1
• Total formula weight: 884.85

Authors

Volpon, L.,Tsan, P.,Besson, F.,Lancelin, J. (deposition date: 2006-09-25, release date: 2006-10-03, Last modification date: 2024-10-30)

Primary citation

Volpon, L.,Tsan, P.,Majer, Z.,Vass, E.,Hollosi, M.,Noguera, V.,Lancelin, J.M.,Besson, F.
NMR Structure Determination of a Synthetic Analogue of Bacillomycin Lc Reveals the Strategic Role of L-Asn1 in the Natural Iturinic Antibiotics.
Spectrochim Acta a Mol.Biomol.Spectrosc., 67:1374-, 2007

PubMed Abstract: Iturins are a group of antifungal produced by Bacillus subtilis. All are cyclic lipopeptides with seven alpha-amino acids of configuration LDDLLDL and one beta-amino fatty acid. The bacillomycin L is a member of this family and its NMR structure was previously resolved using the sequence Asp-Tyr-Asn-Ser-Gln-Ser-Thr. In this work, we carefully examined the NMR spectra of this compound and detected an error in the sequence. In fact, Asp1 and Gln5 need to be changed into Asn1 and Glu5, which therefore makes it identical to bacillomycin Lc. As a consequence, it now appears that all iturinic peptides with antibiotic activity share the common beta-amino fatty acid 8-L-Asn1-D-Tyr2-D-Asn3 sequence. To better understand the conformational influence of the acidic residue L-Asp1, present, for example in the inactive iturin C, the NMR structure of the synthetic analogue SCP [cyclo (L-Asp1-D-Tyr2-D-Asn3-L-Ser4-L-Gln5-D-Ser6-L-Thr7-beta-Ala8)] was determined and compared with bacillomycin Lc recalculated with the corrected sequence. In both cases, the conformers obtained were separated into two families of similar energy which essentially differ in the number and type of turns. A detailed analysis of both cyclopeptide structures is presented here. In addition, CD and FTIR spectra were performed and confirmed the conformational differences observed by NMR between both cyclopeptides.

PubMed: 17129757
DOI: 10.1016/J.SAA.2006.10.027

Experimental method

SOLUTION NMR