Research Articles

Fatty acyl recognition and transfer by an integral membrane S-acyltransferase

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Science  12 Jan 2018:
Vol. 359, Issue 6372, eaao6326
DOI: 10.1126/science.aao6326

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Fattening up proteins

Many eukaryotic proteins are modified by the attachment of lipids, and these modifications can alter how proteins interact with cellular membranes. Rana et al. present x-ray crystal structures of an integral membrane enzyme that appends a fatty acyl chain onto a cysteine residue of target proteins. The enzyme active site is situated at the membrane surface, thus explaining the enzyme's preference for substrates that are already membrane-associated. The structure of a fatty acid-like inhibitor bound within a hydrophobic cavity elucidates the mechanism for the enzyme's acyl chain specificity.

Science, this issue p. eaao6326