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Structural basis for the selectivity of the external thioesterase of the surfactin synthetase
by
Marahiel, Mohamed A
, Dötsch, Volker
, Koglin, Alexander
, Wagner, Gerhard
, Strieter, Eric R
, Frueh, Dominique P
, Walsh, Christopher T
, Rogov, Vladimir V
, Bernhard, Frank
, Mofid, Mohammad R
, Löhr, Frank
, Güntert, Peter
in
Bacillus subtilis
/ Bacillus subtilis - enzymology
/ Bacterial Proteins - biosynthesis
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Biochemistry
/ Enzymes
/ Fatty Acid Synthases - chemistry
/ Fatty Acid Synthases - metabolism
/ Hydrogen bonds
/ Ligases
/ Models, Molecular
/ Molecular structure
/ Nuclear Magnetic Resonance, Biomolecular
/ Peptide Synthases - biosynthesis
/ Peptide Synthases - chemistry
/ Peptide Synthases - metabolism
/ Peptides
/ Protein Interaction Domains and Motifs
/ Protein Structure, Tertiary
/ Surface active agents
/ Thiolester Hydrolases - chemistry
/ Thiolester Hydrolases - metabolism
2008
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Structural basis for the selectivity of the external thioesterase of the surfactin synthetase
by
Marahiel, Mohamed A
, Dötsch, Volker
, Koglin, Alexander
, Wagner, Gerhard
, Strieter, Eric R
, Frueh, Dominique P
, Walsh, Christopher T
, Rogov, Vladimir V
, Bernhard, Frank
, Mofid, Mohammad R
, Löhr, Frank
, Güntert, Peter
in
Bacillus subtilis
/ Bacillus subtilis - enzymology
/ Bacterial Proteins - biosynthesis
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Biochemistry
/ Enzymes
/ Fatty Acid Synthases - chemistry
/ Fatty Acid Synthases - metabolism
/ Hydrogen bonds
/ Ligases
/ Models, Molecular
/ Molecular structure
/ Nuclear Magnetic Resonance, Biomolecular
/ Peptide Synthases - biosynthesis
/ Peptide Synthases - chemistry
/ Peptide Synthases - metabolism
/ Peptides
/ Protein Interaction Domains and Motifs
/ Protein Structure, Tertiary
/ Surface active agents
/ Thiolester Hydrolases - chemistry
/ Thiolester Hydrolases - metabolism
2008
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Structural basis for the selectivity of the external thioesterase of the surfactin synthetase
by
Marahiel, Mohamed A
, Dötsch, Volker
, Koglin, Alexander
, Wagner, Gerhard
, Strieter, Eric R
, Frueh, Dominique P
, Walsh, Christopher T
, Rogov, Vladimir V
, Bernhard, Frank
, Mofid, Mohammad R
, Löhr, Frank
, Güntert, Peter
in
Bacillus subtilis
/ Bacillus subtilis - enzymology
/ Bacterial Proteins - biosynthesis
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Biochemistry
/ Enzymes
/ Fatty Acid Synthases - chemistry
/ Fatty Acid Synthases - metabolism
/ Hydrogen bonds
/ Ligases
/ Models, Molecular
/ Molecular structure
/ Nuclear Magnetic Resonance, Biomolecular
/ Peptide Synthases - biosynthesis
/ Peptide Synthases - chemistry
/ Peptide Synthases - metabolism
/ Peptides
/ Protein Interaction Domains and Motifs
/ Protein Structure, Tertiary
/ Surface active agents
/ Thiolester Hydrolases - chemistry
/ Thiolester Hydrolases - metabolism
2008
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Structural basis for the selectivity of the external thioesterase of the surfactin synthetase
Journal Article
Structural basis for the selectivity of the external thioesterase of the surfactin synthetase
2008
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Overview
Non-ribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) found in bacteria, fungi and plants use two different types of thioesterases for the production of highly active biological compounds. Type I thioesterases (TEI) catalyse the release step from the assembly line of the final product where it is transported from one reaction centre to the next as a thioester linked to a 4′-phosphopantetheine (4′-PP) cofactor that is covalently attached to thiolation (T) domains. The second enzyme involved in the synthesis of these secondary metabolites, the type II thioesterase (TEII), is a crucial repair enzyme for the regeneration of functional 4′-PP cofactors of holo-T domains of NRPS and PKS systems. Mispriming of 4′-PP cofactors by acetyl- and short-chain acyl-residues interrupts the biosynthetic system. This repair reaction is very important, because roughly 80% of CoA, the precursor of the 4′-PP cofactor, is acetylated in bacteria. Here we report the three-dimensional structure of a type II thioesterase from Bacillus subtilis free and in complex with a T domain. Comparison with structures of TEI enzymes shows the basis for substrate selectivity and the different modes of interaction of TEII and TEI enzymes with T domains. Furthermore, we show that the TEII enzyme exists in several conformations of which only one is selected on interaction with its native substrate, a modified holo-T domain.
Publisher
Nature Publishing Group
Subject
/ Bacillus subtilis - enzymology
/ Bacterial Proteins - biosynthesis
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Enzymes
/ Fatty Acid Synthases - chemistry
/ Fatty Acid Synthases - metabolism
/ Ligases
/ Nuclear Magnetic Resonance, Biomolecular
/ Peptide Synthases - biosynthesis
/ Peptide Synthases - chemistry
/ Peptide Synthases - metabolism
/ Peptides
/ Protein Interaction Domains and Motifs
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