Structural and Functional Insights into a Peptide Bond-forming Bidomain from a Nonribosomal Peptide Synthetase.
From: Department of Chemistry/Biochemistry, Philipps-Universität, Hans-Meerwein-Strasse, D-35032 Marburg, Germany.
Structure (London, England : 1993)
- Publish Date: Jul 2007
- ISSN: 0969-2126
- Volume: 15
- Issue: 7
- Pages: 781-92
- Medium: Print
- Language: English
- Citation (JAMA): Samel Stefan A, Schoenafinger Georg, Knappe Thomas A, et al. Structural and Functional Insights into a Peptide Bond-forming Bidomain from a Nonribosomal Peptide Synthetase.. Structure Jul 2007;15:781-92
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.
Mesh Headings (Keywords): Amino Acid Sequence, Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Peptide Synthases, Peptides, Protein Structure, Tertiary, Tandem Mass Spectrometry
Check for Full Text / PubMed Unique Identifier (PMID): 17637339
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