Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects

Bonmatin, Jean‐Marc; Genest, Monique; Petit, Marie-Christine; Gincel, Édith; Simorre, Jean-Pierre; Cornet, Bruno; Gallet, Xavier; Caille, Anita; Labbé, H. J.; Vovelle, F.; Ptak, Marius

doi:10.1016/0300-9084(92)90065-m

Cited by 23 publications

(19 citation statements)

References 42 publications

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“…The reason for this failure to incorporate the other amino acids is not fully understood; however, one likely explanation takes into consideration the complex structure of surfactin. Although its exact conformation has not been precisely determined, two very similar models exist, which describe a``saddle'' topology for the cyclic backbone (Bonmatin et al 1992. There seem to be extensive intramolecular interactions which play an essential role in maintaining the structure of surfactin.…”

Section: Discussionmentioning

confidence: 99%

“…There seem to be extensive intramolecular interactions which play an essential role in maintaining the structure of surfactin. In particular, a hydrogen bond between the Leu2 carbonyl and the Asp5 amide groups stabilizes the b-turn that is characteristic for the structure of surfactin (Bonmatin et al 1992). Several natural amino acid substitutions within the peptide chains of surfactin, as well as other non-ribosomally synthesized peptide antibiotics, have been described, which are due to a reduction in the substrate speci®city of certain modules (Peypoux et al 1994).…”

Section: Discussionmentioning

confidence: 99%

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Targeted alteration of the substrate specificity of peptide synthetases by rational module swapping

1998

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Analysis of the primary structure of peptide synthetases involved in the non-ribosomal synthesis of peptide antibiotics has revealed a highly conserved and ordered modular arrangement. A module contains at least two domains, involved in ATP-dependent substrate activation and thioester formation. The occurrence and arrangement of these functional building blocks is associated with the number and order of the amino acids incorporated in the peptide product. In this study, we present data on the targeted exchange of the leucine-activating module within the three-module surfactin synthetase 1 (SrfA-A) of Bacillus subtilis. This was achieved by engineering several hybrid srfA-A genes, which were introduced into the surfactin biosynthesis operon by in vivo recombination. We examined the hybrid genes for expression and investigated the enzymatic activities of the resulting recombinant peptide synthetases. For the first time, we demonstrate directly that an individual minimal module, of bacterial or fungal origin, confers its amino acid-specific activity on a multi-modular peptide synthetase. Furthermore, it is shown that directed incorporation of ornithine at the second position of the peptide chain induces a global alteration in the conformation of surfactin and may result in premature cyclization or a branched cyclic structure.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Targeted alteration of the substrate specificity of peptide synthetases by rational module swapping

1998

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“…To contribute to a better understanding of the role of each residue in surfactins, our results can be analyzed in the light of the 3D solution structure of surfactin from NMR data [12,19]. Such an approach is justified, since we have studied the Leu 4 and Ile 4 variants and surfactin under the same experimental conditions.…”

Section: Discussionmentioning

confidence: 99%

Production, isolation and characterization of [Leu4]- and [Ile4]surfactins from Bacillus subtilis

et al. 1995

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Bacillus subtilis coproduces several surfactin variants that are powerful biosurfactants and have potential applications in biology and industry. A single amino acid substitution in the heptapeptide moiety of surfaetins strongly modifies their properties. To better establish structure-activity relationships and to search new variants with enhanced properties, Bacillus subtilis was grown into two modified culture media. Two new variants were isolated by chromatographic methods and studied by NMR spectroscopy. As planned, modifications consisted in the substitution of the L-valine residue at the fourth position by a more hydrophobic residue, i.e., leucine or isoleucine. These [Leu4]-and [Ile4]surfactins have a higher affinity for hydrophobic solvents and a twice improved surfactant power. Structure-property correlations were confirmed by analysis of the hydrophobic residue distribution in the three-dimensional model of the structure of surfactin in solution.

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“…The cyclic peptide adopts a horse-saddle structure in solution with the two carboxylic acids as the hydrophilic parts 5,6 .…”

Section: A Is a Promising Bs Produced By Various Strains Of Bacillus mentioning

confidence: 99%

Monolayer Behavior of Cyclic and Linear Forms of Surfactins: Thermodynamic Analysis of Langmuir Monolayers and AFM Study of Langmuir-Blodgett Monolayers

Taira¹,

Ikeda

Kawamura

et al. 2014

J. Oleo Sci.

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Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects

Cited by 23 publications

References 42 publications

Targeted alteration of the substrate specificity of peptide synthetases by rational module swapping

Targeted alteration of the substrate specificity of peptide synthetases by rational module swapping

Production, isolation and characterization of [Leu4]- and [Ile4]surfactins from Bacillus subtilis

Monolayer Behavior of Cyclic and Linear Forms of Surfactins: Thermodynamic Analysis of Langmuir Monolayers and AFM Study of Langmuir-Blodgett Monolayers

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