LAUSR.org creates dashboard-style pages of related content for over 1.5 million academic articles. Sign Up to like articles & get recommendations!

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

Photo by asfotosde1enorme from unsplash

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… Click to show full 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).

Keywords: osacbp2; c18 coa; acyl coa; coa; coa binding

Journal Title: FEBS Letters
Year Published: 2020

Link to full text (if available)


Share on Social Media:                               Sign Up to like & get
recommendations!

Related content

More Information              News              Social Media              Video              Recommended



                Click one of the above tabs to view related content.