6BML
Structure of human DHHC20 palmitoyltransferase, irreversibly inhibited by 2-bromopalmitate
Summary for 6BML
| Entry DOI | 10.2210/pdb6bml/pdb |
| Descriptor | human DHHC20 palmitoyltransferase, ZINC ION, PALMITIC ACID, ... (6 entities in total) |
| Functional Keywords | dhhc, lipid, acyl, palmitoyltransferase., transferase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Membrane ; Multi-pass membrane protein : Q5W0Z9 |
| Total number of polymer chains | 2 |
| Total formula weight | 70671.87 |
| Authors | Rana, M.S.,Lee, C.-J.,Banerjee, A. (deposition date: 2017-11-15, release date: 2018-01-24, Last modification date: 2024-12-25) |
| 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 Cited by 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: 29326245DOI: 10.1126/science.aao6326 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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