5w7i

X-ray structure of ankyrin repeat domain of DHHC17 in complex with Snap25b peptide

spinqualitylabelsall models 5w7i, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5w7i is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Protein S-acyltransferase, with EC number 2.3.1.225 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ZDH17_HUMAN] Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD. Palmitoylates MPP1 in erythrocytes. May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane. Has transforming activity. Mediates Mg(2+) transport. Publication Abstract from PubMed DHHC enzymes catalyze palmitoylation, a major post-translational modification that regulates a number of key cellular processes. There are up to 24 DHHCs in mammals and hundreds of substrate proteins that get palmitoylated. However, how DHHC enzymes engage with their substrates is still poorly understood. There is currently no structural information about the interaction between any DHHC enzyme and protein substrates. In this study we have investigated the structural and thermodynamic bases of interaction between the ankyrin repeat domain of human DHHC17 (ANK17) and Snap25b. We solved a high-resolution crystal structure of the complex between ANK17 and a peptide fragment of Snap25b. Through structure-guided mutagenesis, we discovered key residues in DHHC17 that are critically important for interaction with Snap25b. We further extended our finding by showing that the same residues are also crucial for the interaction of DHHC17 with Huntingtin, one of its most physiologically relevant substrates. Structural Basis for Substrate Recognition by the Ankyrin Repeat Domain of Human DHHC17 Palmitoyltransferase.,Verardi R, Kim JS, Ghirlando R, Banerjee A Structure. 2017 Jul 18. pii: S0969-2126(17)30214-9. doi:, 10.1016/j.str.2017.06.018. PMID:28757145 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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