2JGP

Structure of the TycC5-6 PCP-C bidomain of the tyrocidine synthetase TycC

Summary for 2JGP

• Entry DOI: 10.2210/pdb2jgp/pdb
• Related: 1DNY
• Descriptor: TYROCIDINE SYNTHETASE 3, SULFATE ION, 1,4-DIETHYLENE DIOXIDE, ... (5 entities in total)
• Functional Keywords: multifunctional enzyme, antibiotic biosynthesis, condensation domain, peptide bond formation, ligase, tyrocidine, antibiotics, phosphopantetheine, nonribosomal peptide synthetase, peptidyl carrier domain
• Biological source: BREVIBACILLUS BREVIS
• Total number of polymer chains: 1
• Total formula weight: 59295.73

Authors

Samel, S.A.,Schoenafinger, G.,Knappe, T.A.,Marahiel, M.A.,Essen, L.-O. (deposition date: 2007-02-13, release date: 2007-10-30, Last modification date: 2024-05-08)

Primary citation

Samel, S.A.,Schoenafinger, G.,Knappe, T.A.,Marahiel, M.A.,Essen, L.-O.
Structural and Functional Insights Into a Peptide Bond-Forming Bidomain from a Nonribosomal Peptide Synthetase.
Structure, 15:781-, 2007

PubMed Abstract: The crystal structure of the bidomain PCP-C from modules 5 and 6 of the nonribosomal tyrocidine synthetase TycC was determined at 1.8 A resolution. The bidomain structure reveals a V-shaped condensation domain, the canyon-like active site groove of which is associated with the preceding peptidyl carrier protein (PCP) domain at its donor side. The relative arrangement of the PCP and the peptide bond-forming condensation (C) domain places the active sites approximately 50 A apart. Accordingly, this PCP-C structure represents a conformational state prior to peptide transfer from the donor-PCP to the acceptor-PCP domain, implying the existence of additional states of PCP-C domain interaction during catalysis. Additionally, PCP-C exerts a mode of cyclization activity that mimics peptide bond formation catalyzed by C domains. Based on mutational data and pK value analysis of active site residues, it is suggested that nonribosomal peptide bond formation depends on electrostatic interactions rather than on general acid/base catalysis.

PubMed: 17637339
DOI: 10.1016/J.STR.2007.05.008

Experimental method

X-RAY DIFFRACTION (1.85 Å)