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Publication Abstract from PubMed

DHHC (Asp-His-His-Cys) palmitoyltransferases are eukaryotic integral membrane enzymes that catalyze protein palmitoylation, which is important in a range of physiological processes, including small guanosine triphosphatase (GTPase) signaling, cell adhesion, and neuronal receptor scaffolding. We present crystal structures of two DHHC palmitoyltransferases and a covalent intermediate mimic. The active site resides at the membrane-cytosol interface, which allows the enzyme to catalyze thioester-exchange chemistry by using fatty acyl-coenzyme A and explains why membrane-proximal cysteines are candidates for palmitoylation. The acyl chain binds in a cavity formed by the transmembrane domain. We propose a mechanism for acyl chain-length selectivity in DHHC enzymes on the basis of cavity mutants with preferences for shorter and longer acyl chains.

Fatty acyl recognition and transfer by an integral membrane S-acyltransferase.,Rana MS, Kumar P, Lee CJ, Verardi R, Rajashankar KR, Banerjee A Science. 2018 Jan 12;359(6372). pii: 359/6372/eaao6326. doi:, 10.1126/science.aao6326. PMID:29326245^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.