Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis

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

Research output: Contribution to journalReview article

65 Scopus citations

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
Publication statusPublished - Dec 19 2006
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

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