Journal
SCIENCE
Volume 359, Issue 6372, Pages 176-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aao6326
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Funding
- Intramural Research Program of the NIH
- National Institutes of Child Health and Human Development [1ZIAHD008928]
- National Institute of Neurological Disorders and Stroke
- National Institute of General Medical Sciences from the NIH [P41 GM103403]
- NIH-ORIP HEI grant [S10RR029205]
- National Cancer Institute [ACB-12002]
- National Institute of General Medical Sciences [AGM-12006]
- NIH, Office of Research Infrastructure Programs, High-End Instrumentation Grant [1S10OD012289-01A1]
- DOE Office of Science [DE-AC02-06CH11357]
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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.
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