Structural highlights
6bms is a 2 chain structure with sequence from Brachidanio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Ligands: | , , , , |
| Gene: | zdhhc15b (Brachidanio rerio) |
| Activity: | Protein S-acyltransferase, with EC number 2.3.1.225 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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.
References
- ↑ Rana MS, Kumar P, Lee CJ, Verardi R, Rajashankar KR, Banerjee A. Fatty acyl recognition and transfer by an integral membrane S-acyltransferase. Science. 2018 Jan 12;359(6372). pii: 359/6372/eaao6326. doi:, 10.1126/science.aao6326. PMID:29326245 doi:http://dx.doi.org/10.1126/science.aao6326
