1QR0

CRYSTAL STRUCTURE OF THE 4'-PHOSPHOPANTETHEINYL TRANSFERASE SFP-COENZYME A COMPLEX

Summary for 1QR0

• Entry DOI: 10.2210/pdb1qr0/pdb
• Descriptor: 4'-PHOSPHOPANTETHEINYL TRANSFERASE SFP, MAGNESIUM ION, COENZYME A, ... (4 entities in total)
• Functional Keywords: protein-coenzyme a complex, transferase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 27334.94

Authors

Reuter, K.,Mofid, R.M.,Marahiel, A.M.,Ficner, R. (deposition date: 1999-06-17, release date: 1999-12-10, Last modification date: 2024-02-14)

Primary citation

Reuter, K.,Mofid, M.R.,Marahiel, M.A.,Ficner, R.
Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily.
EMBO J., 18:6823-6831, 1999

PubMed Abstract: 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.

PubMed: 10581256
DOI: 10.1093/emboj/18.23.6823

Experimental method

X-RAY DIFFRACTION (1.9 Å)