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Structure and Substrate Sequestration in the Pyoluteorin Type II Peptidyl Carrier Protein PltL.

Type II nonribosomal peptide synthetases (NRPS) generate exotic amino acid derivatives that, combined with additional pathways, form many bioactive natural products. One family of type II NRPSs produce pyrrole moieties, which commonly arise from proline oxidation while tethered to a conserved, type... Full description

Journal Title: Journal of the American Chemical Society September 16, 2015, Vol.137(36), pp.11546-11549
Main Author: Jaremko, Matt J
Other Authors: Lee, D John , Opella, Stanley J , Burkart, Michael D
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1520-5126 ; DOI: 1520-5126 ; DOI: 10.1021/jacs.5b04525
Link: http://search.proquest.com/docview/1713526765/?pq-origsite=primo
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recordid: proquest1713526765
title: Structure and Substrate Sequestration in the Pyoluteorin Type II Peptidyl Carrier Protein PltL.
format: Article
creator:
  • Jaremko, Matt J
  • Lee, D John
  • Opella, Stanley J
  • Burkart, Michael D
subjects:
  • Magnetic Resonance Spectroscopy–Chemistry
  • Models, Molecular–Chemistry
  • Phenols–Chemistry
  • Phospholipid Transfer Proteins–Chemistry
  • Protein Conformation–Chemistry
  • Pyrroles–Chemistry
  • Phenols
  • Phospholipid Transfer Proteins
  • Pyrroles
  • Pyoluteorin
ispartof: Journal of the American Chemical Society, September 16, 2015, Vol.137(36), pp.11546-11549
description: Type II nonribosomal peptide synthetases (NRPS) generate exotic amino acid derivatives that, combined with additional pathways, form many bioactive natural products. One family of type II NRPSs produce pyrrole moieties, which commonly arise from proline oxidation while tethered to a conserved, type II peptidyl carrier protein (PCP), as exemplified by PltL in the biosynthesis of pyoluteorin. We sought to understand the structural role of pyrrole PCPs in substrate and protein interactions through the study of pyrrole analogs tethered to PltL. Solution-phase NMR structural analysis revealed key interactions in residues of helix II and III with a bound pyrrole moiety. Conservation of these residues among PCPs in other pyrrole containing pathways suggests a conserved mechanism for formation, modification, and incorporation of pyrrole moieties. Further NOE analysis provided a unique pyrrole binding motif, offering accurate substrate positioning within the cleft between helices II and III. The overall structure resembles other PCPs but contains a unique conformation for helix III. This provides evidence of sequestration by the PCP of aromatic pyrrole substrates, illustrating the importance of substrate protection and regulation in type II NRPS systems.
language: eng
source:
identifier: E-ISSN: 1520-5126 ; DOI: 1520-5126 ; DOI: 10.1021/jacs.5b04525
fulltext: no_fulltext
issn:
  • 15205126
  • 1520-5126
url: Link


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titleStructure and Substrate Sequestration in the Pyoluteorin Type II Peptidyl Carrier Protein PltL.
creatorJaremko, Matt J ; Lee, D John ; Opella, Stanley J ; Burkart, Michael D
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subjectMagnetic Resonance Spectroscopy–Chemistry ; Models, Molecular–Chemistry ; Phenols–Chemistry ; Phospholipid Transfer Proteins–Chemistry ; Protein Conformation–Chemistry ; Pyrroles–Chemistry ; Phenols ; Phospholipid Transfer Proteins ; Pyrroles ; Pyoluteorin
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descriptionType II nonribosomal peptide synthetases (NRPS) generate exotic amino acid derivatives that, combined with additional pathways, form many bioactive natural products. One family of type II NRPSs produce pyrrole moieties, which commonly arise from proline oxidation while tethered to a conserved, type II peptidyl carrier protein (PCP), as exemplified by PltL in the biosynthesis of pyoluteorin. We sought to understand the structural role of pyrrole PCPs in substrate and protein interactions through the study of pyrrole analogs tethered to PltL. Solution-phase NMR structural analysis revealed key interactions in residues of helix II and III with a bound pyrrole moiety. Conservation of these residues among PCPs in other pyrrole containing pathways suggests a conserved mechanism for formation, modification, and incorporation of pyrrole moieties. Further NOE analysis provided a unique pyrrole binding motif, offering accurate substrate positioning within the cleft between helices II and III. The overall structure resembles other PCPs but contains a unique conformation for helix III. This provides evidence of sequestration by the PCP of aromatic pyrrole substrates, illustrating the importance of substrate protection and regulation in type II NRPS systems.
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