6BMS

Palmitoyltransferase structure

Summary for 6BMS

• Entry DOI: 10.2210/pdb6bms/pdb
• Descriptor: Palmitoyltransferase, ZINC ION, DODECYL-BETA-D-MALTOSIDE, ... (7 entities in total)
• Functional Keywords: membrane bound enzyme, membrane protein
• Biological source: Danio rerio (Zebrafish)
• Total number of polymer chains: 2
• Total formula weight: 83740.35

Authors

Kumar, P.,Rajashankar, K. (deposition date: 2017-11-15, release date: 2018-01-10, Last modification date: 2024-03-13)

Primary citation

Rana, M.S.,Kumar, P.,Lee, C.J.,Verardi, R.,Rajashankar, K.R.,Banerjee, A.
Fatty acyl recognition and transfer by an integral membraneS-acyltransferase.
Science, 359:-, 2018

PubMed Abstract: 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.

PubMed: 29326245
DOI: 10.1126/science.aao6326

Experimental method

X-RAY DIFFRACTION (2.441 Å)