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Introduction

      Sterol O-acyltransferase(SOAT), otherwise known as Acyl-coenzyme A:cholesterol acyltransferase(ACAT), is the founding member of the membrane-bound O-acyl transferase(MBOAT) enzyme family. MBOAT enzymes transfer acyl chains onto various substrates, including lipids, peptides, and small proteins. There are 11 MBOAT family members in humans, which participate in a variety of physiological processes.
      SOAT specifically catalyzes the esterification of cholesterol for efficient storage within the cell. Cholesterol is a membrane lipid that plays an essential role in maintaining the fluidity and integrity of the membrane, and cholesteryl esters are formed when an excess of cholesterol is present. 

Structure

      The overall structure of the enzyme is a tetramer structure or a dimer of dimers. The functional building block of SOAT is a dimer which is made up of two identical monomer structures. The residues that form the dimer interface are mostly hydrophobic and interact with each other in a shape-complementary manner. Mutating residues within the dimer interface reduced the dimers to monomer fractions, indicating that the dimeric architecture is important for the activity of the enzyme. The dimerization of SOAT is mainly mediated by extensive van der Waals interactions between TM1 in one protomer and the lumenal segment of TM6 and the cytosolic segment of TM9 in the other. TM1, TM5, TM6 and TM9 from the two protomers enclose a deep hydrophobic pocket that is open to the lumenal side. Numerous hydrophobic residues on TM6 and TM9 from one protomer contact those on TM1 from the other protomer. On the intracellular side, hydrophobic residues on IH1 of each protomer interact with each other to stabilize the dimer. 

Active Site

Function

Disease

Relevance

Structural highlights

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