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UID:20250816T120854EDT-43689uVoxT@132.216.98.100
DTSTAMP:20250816T160854Z
DESCRIPTION:Nonribosomal peptide synthetases (NRPSs) are microbial enzymati
 c systems that synthesize a wealth of important natural products such as v
 irulence factors (e.g. yersiniabactin) or antibiotics (penicillin\, vancom
 ycin). NRPSs employ conserved domains to tether simple substrates via thio
 ester bonds and condense them into complex natural products via peptide bo
 nds. Recent studies showed that NRPSs are not rigid but undergo a series o
 f sequential\, transient molecular interactions during synthesis. Nuclear 
 magnetic resonance (NMR) is ideally suited for studies of such dynamic pro
 teins and for characterizing transient interactions\, but the method is of
 ten limited to proteins smaller than many NRPS domains. Here\, we showcase
  the molecular information provided by NMR with studies of small NRPS carr
 ier proteins\, and we describe NMR methods to overcome challenges in studi
 es of larger proteins.\n\nWe present the first structure of an NRPS carrie
 r protein covalently attached to its substrate via a labile thioester bond
 . We show that the substrate interacts with the protein core\, albeit in a
  transient manner. This interaction modulates protein dynamics and alters 
 surfaces involved in molecular binding. Our observations provide a molecul
 ar basis for interplay between the successive chemical reactions that occu
 r in NRPS synthesis and related domain communication.\n\nNMR resonances as
 signment is a major bottle neck for studies of larger proteins.  To assign
  NMR signals\, investigators must analyze a series of spectra and identify
  signals that belong to sequential residues\, and this protocol becomes ex
 ponentially more difficult as the number of residues increases. We have tr
 anslated this procedure into mathematical operations that can be applied t
 o NMR spectra. Thus\, a single correlation map harnesses the information o
 f all data collected\, and resonance assignment is obtained by visual insp
 ection. The method is illustrated for assignment of backbone and side-chai
 n resonances of 37 kDa and 52 kDa NRPS domains.\n
DTSTART:20151027T050000Z
DTEND:20151027T063000Z
LOCATION:Room 10\, Maass Chemistry Building\, CA\, QC\, Montreal\, H3A 0B8\
 , 801 rue Sherbrooke Ouest
SUMMARY:Chemical Society: Dr. Dominique Frueh - NMR studies of nonribosomal
  peptide synthetases. Pushing the frontiers of NMR.
URL:/chemistry/channels/event/chemical-society-dr-domi
 nique-frueh-nmr-studies-nonribosomal-peptide-synthetases-pushing-frontiers
 -256218
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