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TitleStructural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 2478, Year 2020
Publish dateMay 18, 2020
AuthorsChengcheng Guan / Yange Niu / Si-Cong Chen / Yunlu Kang / Jing-Xiang Wu / Koji Nishi / Catherine C Y Chang / Ta-Yuan Chang / Tuoping Luo / Lei Chen /
PubMed AbstractSterol O-acyltransferase 1 (SOAT1) is an endoplasmic reticulum (ER) resident, multi-transmembrane enzyme that belongs to the membrane-bound O-acyltransferase (MBOAT) family. It catalyzes the ...Sterol O-acyltransferase 1 (SOAT1) is an endoplasmic reticulum (ER) resident, multi-transmembrane enzyme that belongs to the membrane-bound O-acyltransferase (MBOAT) family. It catalyzes the esterification of cholesterol to generate cholesteryl esters for cholesterol storage. SOAT1 is a target to treat several human diseases. However, its structure and mechanism remain elusive since its discovery. Here, we report the structure of human SOAT1 (hSOAT1) determined by cryo-EM. hSOAT1 is a tetramer consisted of a dimer of dimer. The structure of hSOAT1 dimer at 3.5 Å resolution reveals that a small molecule inhibitor CI-976 binds inside the catalytic chamber and blocks the accessibility of the active site residues H460, N421 and W420. Our results pave the way for future mechanistic study and rational drug design targeting hSOAT1 and other mammalian MBOAT family members.
External linksNat Commun / PubMed:32424158 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 8.25 Å
Structure data

EMDB-0829:
Structure of the human sterol O-acyltransferase 1 tetramer in oval shape
Method: EM (single particle) / Resolution: 8.25 Å

EMDB-0830:
Structure of the human sterol O-acyltransferase 1 tetramer in rhombic shape
Method: EM (single particle) / Resolution: 7.6 Å

0831

6l47

EMDB-0831, PDB-6l47:
Structure of the human sterol O-acyltransferase 1 in complex with CI-976
Method: EM (single particle) / Resolution: 3.5 Å

0832

6l48

EMDB-0832, PDB-6l48:
Structure of the human sterol O-acyltransferase 1 in resting state
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-E5L:
2,2-dimethyl-N-(2,4,6-trimethoxyphenyl)dodecanamide

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / TRANSFERASE / SOAT / ACAT / MBOAT

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