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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Piecing together nonribosomal peptide synthesis.

Janice M Reimer1, Asfarul S Haque1, Michael J Tarry1

  • 1Department of Biochemistry, McGill University, Montréal, QC H3G 0B1, Canada.

Current Opinion in Structural Biology
|February 15, 2018
PubMed
Summary
This summary is machine-generated.

Nonribosomal peptide synthetases (NRPSs) are complex enzymes. Recent structural studies reveal the architecture and dynamics of these megaenzymes, advancing our understanding of NRPS assembly-line logic.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Nonribosomal peptide synthetases (NRPSs) are large enzyme complexes responsible for synthesizing a diverse array of bioactive peptides.
  • NRPSs function via a modular assembly-line mechanism, with each module incorporating specific building blocks and performing catalytic modifications.
  • Determining the structures of large NRPS assemblies has been challenging, limiting a comprehensive understanding of their architecture and function.

Purpose of the Study:

  • To review recent advancements in the structural determination of multi-domain NRPS proteins.
  • To integrate new structural data with existing knowledge to provide a holistic view of NRPS megaenzyme architecture.
  • To elucidate domain-domain interactions and conformational changes critical for NRPS catalytic cycles.

Main Methods:

  • Structure determination of four multi-domain NRPS proteins, including initiation and termination modules, and a cross-module construct.
  • Analysis of novel didomain NRPS structures.
  • Integration of structural data to understand NRPS assembly, interactions, and dynamics.

Main Results:

  • Successful structure determination of key multi-domain NRPS components, overcoming previous limitations.
  • Insights into the structural basis of initiation and termination steps in NRPS pathways.
  • Elucidation of domain-domain interfaces and their role in conformational flexibility and catalysis.

Conclusions:

  • Recent structural breakthroughs provide unprecedented insights into the architecture and operational mechanisms of NRPS megaenzymes.
  • Understanding NRPS structure is crucial for deciphering their complex catalytic cycles and domain interactions.
  • These findings advance the field of NRPS research, paving the way for future studies on NRPS assembly and function.