Structural characterization of three noncanonical NTF2‐like superfamily proteins: implications for polyketide biosynthesis. Issue 8 (3rd August 2020)

• Record Type: Journal Article
• Authors: Vuksanovic, Nemanja; Zhu, Xuechen; Serrano, Dante A.; Siitonen, Vilja; Metsä-Ketelä, Mikko; Melançon, Charles E.; Silvaggi, Nicholas R.
• Is Part Of: Acta crystallographica. Volume 76:Issue 8(2020:Aug.)
• Page Start: 372
• Page End: 383
• Publication Date: 2020-08-03
• Subjects: NTF2‐like superfamily -- polyketide cyclases -- actinorhodin -- alnumycin -- secondary metabolism; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X20009814
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The structures of three closely related NTF2‐like superfamily proteins that are involved in type II polyketide biosynthesis in as‐yet‐unknown ways were determined. The presence of a solvent‐accessible cavity and the conservation of the His/Asp dyad suggest a potential enzymatic role for these enzymes in polyketide biosynthesis. 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.