A nuclear magnetic resonance method for probing molecular influences of substrate loading in nonribosomal peptide synthetase carrier proteins

Andrew C. Goodrich, Dominique P. Frueh

Research output: Contribution to journalArticle

Abstract

Carrier proteins (CPs) play a central role in nonribosomal peptide synthetases (NRPSs) as they shuttle covalently attached substrates between active sites. Understanding how the covalent attachment of a substrate (loading) influences the molecular properties of CPs is key to determining the mechanism of NRPS synthesis. However, structural studies have been impaired by substrate hydrolysis. Here, we used nuclear magnetic resonance spectroscopy to monitor substrate loading of a CP and to overcome hydrolysis. Our results reveal the spectroscopic signature of substrate loading and provide evidence of molecular communication between an NRPS carrier protein and its covalently attached substrate.

LanguageEnglish (US)
Pages1154-1156
Number of pages3
JournalBiochemistry®
Volume54
Issue number5
DOIs
StatePublished - Feb 10 2015

Fingerprint

Peptide Synthases
Carrier Proteins
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Substrates
Hydrolysis
Catalytic Domain
Nuclear magnetic resonance spectroscopy
Communication

ASJC Scopus subject areas

  • Biochemistry

Cite this

A nuclear magnetic resonance method for probing molecular influences of substrate loading in nonribosomal peptide synthetase carrier proteins. / Goodrich, Andrew C.; Frueh, Dominique P.

In: Biochemistry®, Vol. 54, No. 5, 10.02.2015, p. 1154-1156.

Research output: Contribution to journalArticle

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