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Title
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Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily.
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Authors
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K.Reuter,
M.R.Mofid,
M.A.Marahiel,
R.Ficner.
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Ref.
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EMBO J, 1999,
18,
6823-6831.
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PubMed id
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Abstract
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The Bacillus subtilis Sfp protein activates the peptidyl carrier protein (PCP)
domains of surfactin synthetase by transferring the 4'-phosphopantetheinyl
moiety of coenzyme A (CoA) to a serine residue conserved in all PCPs. Its wide
PCP substrate spectrum renders Sfp a biotechnologically valuable enzyme for use
in combinatorial non-ribosomal peptide synthesis. The structure of the Sfp-CoA
complex determined at 1.8 A resolution reveals a novel alpha/beta-fold
exhibiting an unexpected intramolecular 2-fold pseudosymmetry. This suggests a
similar fold and dimerization mode for the homodimeric phosphopantetheinyl
transferases such as acyl carrier protein synthase. The active site of Sfp
accommodates a magnesium ion, which is complexed by the CoA pyrophosphate, the
side chains of three acidic amino acids and one water molecule. CoA is bound in
a fashion that differs in many aspects from all known CoA-protein complex
structures. The structure reveals regions likely to be involved in the
interaction with the PCP substrate.
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