Structural characterization of three noncanonical NTF2-like superfamily proteins: implications for polyketide biosynthesis - UTU Research Portal

A1 Refereed original research article in a scientific journal

Structural characterization of three noncanonical NTF2-like superfamily proteins: implications for polyketide biosynthesis

Authors: N. Vuksanovic, X. Zhu, D.A. Serrano, V. Siitonen, M. Metsä-Ketelä, C.E. Melancon III, N.R. Silvaggi

Publisher: INT UNION CRYSTALLOGRAPHY

Publication year: 2020

Journal: Acta Crystallographica Section F: Structural Biology Communications

Journal name in source: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS

Journal acronym: ACTA CRYSTALLOGR F

Volume: 76

First page : 372

Last page: 383

Number of pages: 12

eISSN: 2053-230X

DOI: https://doi.org/10.1107/S2053230X20009814

Self-archived copy’s web address: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397469

Abstract

Proteins belonging to the NTF2-like superfamily are present in the biosynthetic pathways of numerous polyketide natural products, such as anthracyclins and benzoisochromanequinones. Some have been found to be bona fide polyketide cyclases, but many of them have roles that are currently unknown. Here, the X-ray crystal structures of three NTF2-like proteins of unknown function are reported: those of ActVI-ORFA from Streptomyces coelicolor A3(2) and its homologs Caci_6494, a protein from an uncharacterized biosynthetic cluster in Catenulispora acidiphila, and Aln2 from Streptomyces sp. CM020, a protein in the biosynthetic pathway of alnumycin. The presence of a solvent-accessible cavity and the conservation of the His/Asp dyad that is characteristic of many polyketide cyclases suggest a potential enzymatic role for these enzymes in polyketide biosynthesis.