Substrate and product complexes reveal mechanisms of Hedgehog acylation by HHAT
Copyright policy )Substrate and product complexes reveal mechanisms of Hedgehog acylation by HHAT
How Hedgehog gets its lipid tail Phospholipid membranes serve as barriers between different cellular environments but are also crucial platforms for biosynthesis, signaling, and transport. In animals, the developmental signaling protein Hedgehog must be modified with an acyl group by the membrane-embedded enzyme Hedgehog acyltransferase (HHAT) to be recognized by its receptor. Using cryo–electron microscopy, Jiang et al. determined structures of HHAT bound to palmitoyl–coenzyme A or a palmitoylated peptide product. Two cavities connect at the active site, enabling acylation of Hedgehog in the lumen of the endoplasmic reticulum by lipid substrates from the cytosolic face of the membrane. Science , abg4998, this issue p. 1215
- Memorial Sloan Kettering Cancer Center United States
Models, Molecular, Palmitoyl Coenzyme A, Acylation, Lipoylation, Cryoelectron Microscopy, Intracellular Membranes, Molecular Dynamics Simulation, Endoplasmic Reticulum, Peptide Fragments, Protein Structure, Secondary, Catalytic Domain, Biocatalysis, Humans, Hedgehog Proteins, Protein Interaction Domains and Motifs, Protein Processing, Post-Translational, Acyltransferases
Models, Molecular, Palmitoyl Coenzyme A, Acylation, Lipoylation, Cryoelectron Microscopy, Intracellular Membranes, Molecular Dynamics Simulation, Endoplasmic Reticulum, Peptide Fragments, Protein Structure, Secondary, Catalytic Domain, Biocatalysis, Humans, Hedgehog Proteins, Protein Interaction Domains and Motifs, Protein Processing, Post-Translational, Acyltransferases
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