Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis

Jonathan R. Lai, Alexander Koglin, Christopher T. Walsh

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Carrier proteins, 80-100 residues in length, serve as information-rich platforms to present growing acyl and peptidyl chains as covalently tethered phosphopantetheinyl-thioester intermediates during the biosynthesis of fatty acid, polyketide, and nonribosomal natural products. Carrier proteins are recognized both in cis and in trans by partner catalytic domains that effect chain-elongating condensations, redox adjustments, other tailoring steps, and finally kinetically controlled disconnection and release of the mature natural product. Dissection of regions of carrier proteins that are specifically recognized by upstream and downstream catalytic partner proteins is deciphering the logic for multiprotein assembly line construction of these large classes of natural products.

Original languageEnglish (US)
Pages (from-to)14869-14879
Number of pages11
JournalBiochemistry
Volume45
Issue number50
DOIs
StatePublished - Dec 19 2006
Externally publishedYes

Fingerprint

Nucleic Acid-Independent Peptide Biosynthesis
Polyketides
Biosynthesis
Biological Products
Carrier Proteins
Peptides
Dissection
Oxidation-Reduction
Condensation
Catalytic Domain
Fatty Acids
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis. / Lai, Jonathan R.; Koglin, Alexander; Walsh, Christopher T.

In: Biochemistry, Vol. 45, No. 50, 19.12.2006, p. 14869-14879.

Research output: Contribution to journalArticle

Lai, Jonathan R. ; Koglin, Alexander ; Walsh, Christopher T. / Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis. In: Biochemistry. 2006 ; Vol. 45, No. 50. pp. 14869-14879.
@article{049229794a534faaa9c25b4c3d8005b1,
title = "Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis",
abstract = "Carrier proteins, 80-100 residues in length, serve as information-rich platforms to present growing acyl and peptidyl chains as covalently tethered phosphopantetheinyl-thioester intermediates during the biosynthesis of fatty acid, polyketide, and nonribosomal natural products. Carrier proteins are recognized both in cis and in trans by partner catalytic domains that effect chain-elongating condensations, redox adjustments, other tailoring steps, and finally kinetically controlled disconnection and release of the mature natural product. Dissection of regions of carrier proteins that are specifically recognized by upstream and downstream catalytic partner proteins is deciphering the logic for multiprotein assembly line construction of these large classes of natural products.",
author = "Lai, {Jonathan R.} and Alexander Koglin and Walsh, {Christopher T.}",
year = "2006",
month = "12",
day = "19",
doi = "10.1021/bi061979p",
language = "English (US)",
volume = "45",
pages = "14869--14879",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "50",

}

TY - JOUR

T1 - Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis

AU - Lai, Jonathan R.

AU - Koglin, Alexander

AU - Walsh, Christopher T.

PY - 2006/12/19

Y1 - 2006/12/19

N2 - Carrier proteins, 80-100 residues in length, serve as information-rich platforms to present growing acyl and peptidyl chains as covalently tethered phosphopantetheinyl-thioester intermediates during the biosynthesis of fatty acid, polyketide, and nonribosomal natural products. Carrier proteins are recognized both in cis and in trans by partner catalytic domains that effect chain-elongating condensations, redox adjustments, other tailoring steps, and finally kinetically controlled disconnection and release of the mature natural product. Dissection of regions of carrier proteins that are specifically recognized by upstream and downstream catalytic partner proteins is deciphering the logic for multiprotein assembly line construction of these large classes of natural products.

AB - Carrier proteins, 80-100 residues in length, serve as information-rich platforms to present growing acyl and peptidyl chains as covalently tethered phosphopantetheinyl-thioester intermediates during the biosynthesis of fatty acid, polyketide, and nonribosomal natural products. Carrier proteins are recognized both in cis and in trans by partner catalytic domains that effect chain-elongating condensations, redox adjustments, other tailoring steps, and finally kinetically controlled disconnection and release of the mature natural product. Dissection of regions of carrier proteins that are specifically recognized by upstream and downstream catalytic partner proteins is deciphering the logic for multiprotein assembly line construction of these large classes of natural products.

UR - http://www.scopus.com/inward/record.url?scp=33845562808&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33845562808&partnerID=8YFLogxK

U2 - 10.1021/bi061979p

DO - 10.1021/bi061979p

M3 - Article

C2 - 17154525

AN - SCOPUS:33845562808

VL - 45

SP - 14869

EP - 14879

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 50

ER -