Acyl carrier protein

spinqualitylabelsall models Structure of E. coli acyl carrier protein complex with thioester, Zn+2 (grey) and Na+ (purple) ions (PDB code 2fad). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Acyl carrier protein (ACP) is a component of the fatty acid biosynthesis cycle. ACP catalyzes the addition of a thioester to a phosphopantetheine moiety. The phosphopantetheine moiety is added post-translationally to ACP serine residue by ACP synthetase (ACPS). The phosphopantetheine contains a free SH group which binds acyl groups in the fatty acid biosynthesis as thioesters. The acyl groups from acetyl-CoA and malonyl-CoA are transferred to ACP. There are 2 types of ACP. ACP I is a multifunctional polypeptide found in yeast and mammals while ACP II is a monomeric protein found in bacteria and plants. See also: Molecular Playground/ACP apo Acyl carrier protein synthase Lipid metabolism Fatty acid synthesis Structural highlights Biological Assembly of E. coli acyl carrier protein (2fad). Active site of E. coli acyl carrier protein. Water molecules are shown as red spheres. The thioester - heptanethioate - is bound to ACP serine residue (colored in darkmagenta) in an expandable hydrophobic cavity. Na coordination site. Active site hydrophobic cavity with thioester heptanethioate. 3D structures of acyl carrier protein Acyl carrier protein 3D structures

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