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PMID: 15582399 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Structural aspects of non-ribosomal peptide biosynthesis.

Current opinion in structural biology ·Vol. 14 ·No. 6 ·2004-12-00 ·Pages 748-56

Challis GL, Naismith JH

Abstract

Small peptides have powerful biological activities ranging from antibiotic to immune suppression. These peptides are synthesized by non-ribosomal peptide synthetases (NRPS). Structural understanding of NRPS took a huge leap forward in 2002; this information has led to several detailed biochemical studies and further structural studies. NRPS are complex molecular machines composed of multiple modules and each module contains several autonomously folded catalytic domains. Structural studies have largely focused on individual domains, isolated from the context of the multienzyme. Biochemical studies have looked at individual domains, isolated whole modules and intact NRPS, and the combined data begin to allow us to visualize the process of peptide assembly by NRPS.

MeSH Terms
Animals Binding Sites Humans Models, Biological Models, Chemical Models, Molecular Peptide Biosynthesis, Nucleic Acid-Independent/physiology Peptides/chemistry,metabolism Protein Binding Protein Conformation Protein Structure, Tertiary Structure-Activity Relationship
Chemicals
Peptides
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Challis Gregory L
Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK.
Naismith James H
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Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
2004-12-00
Pages
748-56
Language
English
Region
England
NLM ID
9107784
PMCID
PMC3326538
Subset
IM
Grants
Biotechnology and Biological Sciences Research Council · BB/H017917/1 · United Kingdom
Biotechnology and Biological Sciences Research Council · BBS/B/14426 · United Kingdom
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