Article
Structural and functional investigation of the intermolecular interaction between NRPS adenylation and carrier protein domains.
Chemistry & biology - 24 Feb 2012
Sundlov Jesse A, Shi Ce, Wilson Daniel J, Aldrich Courtney C, Gulick Andrew M
Abstract excerpt
Nonribosomal peptide synthetases (NRPSs) are modular proteins that produce peptide antibiotics and siderophores. These enzymes act as catalytic assembly lines where substrates, covalently bound to integrated carrier domains, are delivered to adjacent catalytic domains. The carrier domains are initially loaded by adenylation domains, which use two distinct conformations to catalyze sequentially the adenylation of...
Topics
- Computer Simulation
- Crystallography, X-Ray
- Escherichia coli
- Escherichia coli Proteins
- Hydrolases
- Kinetics
- Ligases
- Mutation
- Peptide Synthases
- Protein Structure, Tertiary
- Recombinant Fusion Proteins
- Substrate Specificity