Binding of acyl-CoA substrates in AccA3/AccD4/AccD5/AccE5 causes a ~90 deg. rotation of the uneven 9-stranded (AccA3)4/AccE5 beta-barrel. The rotation propagates into the complete AccA3 assembly, which is split into two asymmetric AccA3 dimers.

A C-terminal helical dimerization module in the AccE5 subunit is responsible for the chimeric assembly of two related acyl-CoA carboxyl transferase subunits (AccD4, AccD5). Each of them specifically catalyzes carboxylation of long-chain and short chain acyl-CoAs, respectively.

Asymmetry, flexibility and sub-complex rotations of the AccA3/AccD4/AccD5/AccE5 holo complex are caused by the presence of a previously unknown epsilon-subunit (AccE5) in red/orange. AccA3, green shades; AccD4, purple shades; AccD5, blue/cyan shades.

We are excited to share our latest work, where we unravel the structural and functional secrets of the once-mysterious protein Pex8 revealing how it controls the peroxisomal cargo import receptor Pex5.

Read more here: www.biorxiv.org/content/10.1101/2025.08.30.673231v1