The abstract is read at the publisher; the summary is JClub's.
Structural snapshots of the KCS6–CER2 complex from Selaginella moellendorffii reveal sequential engagement of C22:0 and malonyl-CoA to form C24:0, plus a new side channel.
- Why it matters: VLCFA elongation is central to plant sphingolipids, phospholipids, triacylglycerols, suberin, and cuticular waxes, yet the catalytic structural mechanism in plants is unclear.
- What they did: The authors solved multiple KCS6–CER2 structures in different elongation reaction states, tracking how behenoyl-CoA, malonyl-CoA, and the C24:0 β-ketoacyl-CoA product occupy the cytosolic substrate channel.
- The result: Structural and biochemical analyses show CER2 functions as a structural cofactor that extends KCS6’s hydrophobic channel and a side channel that accommodates an extra acyl-CoA, enabling chain-length-specific VLCFA elongation.
The findingWhy it mattersWhat they didThe result
AI summary of the abstract · may contain errors · not medical advice · read the paper.