2VSQ

Structure of surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module

Summary for 2VSQ

• Entry DOI: 10.2210/pdb2vsq/pdb
• Related: 1JMK
• Descriptor: SURFACTIN SYNTHETASE SUBUNIT 3, LEUCINE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ligase, peptidyl carrier protein, ligase phosphoprotein, termination module, phosphopantetheine, nonribosomal peptide synthesis, synthetase, adenylation, sporulation, antibiotic biosynthesis, enzymatic assembly line, surfactin a, condensation, thioesterase
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 1
• Total formula weight: 147667.78

Authors

Tanovic, A.,Samel, S.A.,Essen, L.-O.,Marahiel, M.A. (deposition date: 2008-04-29, release date: 2008-07-08, Last modification date: 2023-12-13)

Primary citation

Tanovic, A.,Samel, S.A.,Essen, L.O.,Marahiel, M.A.
Crystal structure of the termination module of a nonribosomal peptide synthetase.
Science, 321:659-663, 2008

PubMed Abstract: Nonribosomal peptide synthetases (NRPSs) are modular multidomain enzymes that act as an assembly line to catalyze the biosynthesis of complex natural products. The crystal structure of the 144-kilodalton Bacillus subtilis termination module SrfA-C was solved at 2.6 angstrom resolution. The adenylation and condensation domains of SrfA-C associate closely to form a catalytic platform, with their active sites on the same side of the platform. The peptidyl carrier protein domain is flexibly tethered to this platform and thus can move with its substrate-loaded 4'-phosphopantetheine arm between the active site of the adenylation domain and the donor side of the condensation domain. The SrfA-C crystal structure has implications for the rational redesign of NRPSs as a means of producing novel bioactive peptides.

PubMed: 18583577
DOI: 10.1126/science.1159850

Experimental method

X-RAY DIFFRACTION (2.6 Å)