8H6S

Structure of acyltransferase VinK in complex with the loading acyl carrier protein of vicenistatin PKS

Summary for 8H6S

• Entry DOI: 10.2210/pdb8h6s/pdb
• Descriptor: Malonyl-CoA-[acyl-carrier-protein] transacylase, Polyketide synthase modules 1-3, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: acyl carrier protein, polyketide synthase, acyltransferase, transferase
• Biological source: Streptomyces halstedii; More
• Total number of polymer chains: 4
• Total formula weight: 106581.03

Authors

Kawada, K.,Miyanaga, A.,Chisuga, T.,Kudo, F.,Eguchi, T. (deposition date: 2022-10-18, release date: 2022-12-21, Last modification date: 2024-11-13)

Primary citation

Miyanaga, A.,Kawada, K.,Chisuga, T.,Kudo, F.,Eguchi, T.
Structural Basis of Transient Interactions of Acyltransferase VinK with the Loading Acyl Carrier Protein of the Vicenistatin Modular Polyketide Synthase.
Biochemistry, 62:17-21, 2023

PubMed Abstract: Acyltransferase (AT) recognizes its cognate acyl carrier protein (ACP) for functional transfer of an acyl unit in polyketide biosynthesis. However, structural characterization of AT-ACP complexes is limited because of the weak and transient interactions between them. In the biosynthesis of macrolactam polyketide vicenistatin, the -acting loading AT VinK transfers a dipeptidyl unit from the stand-alone ACP VinL to the ACP domain (VinP1ACP) of the loading module of modular polyketide synthase VinP1. Although the previously determined structure of the VinK-VinL complex clearly illustrates the VinL recognition mechanism of VinK, how VinK recognizes VinP1ACP remains unclear. Here, the crystal structure of a covalent VinK-VinP1ACP complex formed with a pantetheine-type cross-linking probe is reported at 3.0 Å resolution. The structure of the VinK-VinP1ACP complex provides detailed insights into the transient interactions between VinK and VinP1ACP. The importance of residues in the binding interface was confirmed by site-directed mutational analyses. The binding interface between VinK and VinP1ACP is similar to that between VinK and VinL, although some of the interface residues are different. However, the ACP orientation and interaction mode observed in the VinK-VinP1ACP complex are different from those observed in other AT-ACP complexes such as the disorazole -AT-ACP complex and -AT-ACP complexes of modular polyketide synthases. Thus, AT-ACP binding interface interactions are different in each type of AT-ACP pair.

PubMed: 36512613
DOI: 10.1021/acs.biochem.2c00645

Experimental method

X-RAY DIFFRACTION (3 Å)