Structural highlights
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural and functional insights into a peptide bond-forming bidomain from a nonribosomal peptide synthetase.,Samel SA, Schoenafinger G, Knappe TA, Marahiel MA, Essen LO Structure. 2007 Jul;15(7):781-92. PMID:17637339[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Samel SA, Schoenafinger G, Knappe TA, Marahiel MA, Essen LO. Structural and functional insights into a peptide bond-forming bidomain from a nonribosomal peptide synthetase. Structure. 2007 Jul;15(7):781-92. PMID:17637339 doi:10.1016/j.str.2007.05.008
