Crystal structure of the rice acyl‐CoA‐binding protein OsACBP2 in complex with C18:3‐CoA reveals a novel pattern of binding to acyl‐CoA esters

Abstract

Acyl‐CoA‐binding proteins (ACBPs) are a family of proteins that bind acyl‐CoA esters at a conserved acyl‐CoA‐binding domain. ACBPs maintain intracellular acyl‐CoA pools to regulate lipid metabolism. Here, we report on the structure of rice OsACBP2 in complex with C18:3‐CoA ester. The residues Y33, K34 and K56 of OsACBP2 play a crucial role in binding the CoA group, while residues N23, L27, K52 and Y55 in one molecule of OsACBP2 cooperate with L27, L28, A59 and A62 from another anchoring the fatty acyl group. Multiangle light scattering assays indicate that OsACBP2 binds C18:3‐CoA as a monomer. The first complex structure of a plant ACBP binding with C18:3‐CoA is therefore presented, providing a novel model for the interaction between an acyl‐CoA ester and the acyl‐CoA‐binding domain(s).

Oxylipin signaling in salt-stressed soybean is modulated by ligand-dependent interaction of Class II acyl-CoA-binding proteins with lipoxygenase

“…Similarly, Class II AtACBP2, when complexed with lysophosphatidylcholine, exhibited 10-fold higher affinity for LYSOPL2 interaction via the ANK domain ( Miao et al, 2019 ). Whilst structural biology of plant ACBPs is still in its infancy, we have resolved the first crystal structure of plant ACBPs using the prototypic Class I OsACBP1 and OsACBP2 ( Guo et al, 2017 ; Jin et al, 2020 ). The structure of OsACBP2 liganded with C18:3-CoA deviates from its apo structure and the structure of prototypic human liver ACBP in complex with C14:0-CoA ( Jin et al, 2020 ).…”

“…Whilst structural biology of plant ACBPs is still in its infancy, we have resolved the first crystal structure of plant ACBPs using the prototypic Class I OsACBP1 and OsACBP2 ( Guo et al, 2017 ; Jin et al, 2020 ). The structure of OsACBP2 liganded with C18:3-CoA deviates from its apo structure and the structure of prototypic human liver ACBP in complex with C14:0-CoA ( Jin et al, 2020 ). The distinctive conformational features of an ACBP, when bound with discrete ligands, may govern the subset of its interactors, which may vary constantly with its changing ligand-binding status.…”

In silico Analysis of Acyl-CoA-Binding Protein Expression in Soybean

“…Considering the high homology amongst ACBP amino acid sequences, the 3D structure of the ACB domain in GmACBPs was predicted based on published ACBP structures from other plants or organisms. The structure of ACBPs as of bovine ACBP determined by nuclear magnetic resonance spectroscopy (Andersen et al, 1991), and those from man (Taskinen et al, 2007), Plasmodium falciparum (van Aalten et al, 2001) and rice (Guo et al, 2017;Jin et al, 2020) showed that each ACBP is made of four α-helices displayed in an up-and-down configuration. In rice, the acyl-CoA ester C18:3-CoA was shown to bind to Class I OsACBP2 in a pocket formed by the two helical structures and FIGURE 6 | GmACBP expression profile following cold stress.…”

“…The control (0 h) was not subject to treatment at 4 • C (Robison et al, 2019). the fatty acyl group of the ester was accommodated in the region of hydrophobic residues (Jin et al, 2020).…”

From benzodiazepines to fatty acids and beyond: revisiting the role of ACBP/DBI

“…In addition, multiple transcript variants of human ACBP/DBI have been identified, including three high abundant and eleven low-abundant transcript variants [13][14][15]. The structures of apo-and holo forms of ACBP/DBI from both lower and higher eukaryotic species have been solved by NMR spectroscopy and/or X-ray crystallography showing that its overall structure as a four-a-helix bundle protein is highly evolutionarily conserved [16][17][18][19][20][21][22][23] (Figure 1).…”