4mrt | pdb_00004mrt

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Template:STRUCTURE 4mrt

Structure of the Phosphopantetheine Transferase Sfp in Complex with Coenzyme A and a Peptidyl Carrier Protein

Template:ABSTRACT PUBMED 24704508

Function

[TYCC_BREPA] Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product. [SFP_BACSU] Activates the seven peptidyl carrier protein (PCP) domains of surfactin synthase SRF1/2/3 by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue. Required for cells of B.subtilis to become producers of the lipopeptide antibiotics surfactin and plipastatin B1.[1]

About this Structure

4mrt is a 2 chain structure. Full crystallographic information is available from OCA.

Reference

  1. Tufar P, Rahighi S, Kraas FI, Kirchner DK, Lohr F, Henrich E, Kopke J, Dikic I, Guntert P, Marahiel MA, Dotsch V. Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification. Chem Biol. 2014 Apr 2. pii: S1074-5521(14)00073-8. doi:, 10.1016/j.chembiol.2014.02.014. PMID:24704508 doi:https://dx.doi.org/10.1016/j.chembiol.2014.02.014
  1. ↑ Lambalot RH, Gehring AM, Flugel RS, Zuber P, LaCelle M, Marahiel MA, Reid R, Khosla C, Walsh CT. A new enzyme superfamily - the phosphopantetheinyl transferases. Chem Biol. 1996 Nov;3(11):923-36. PMID:8939709

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