Asset Details
Do you wish to reserve the book?
Structure and mechanism of human diacylglycerol O-acyltransferase 1
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structure and mechanism of human diacylglycerol O-acyltransferase 1
Do you wish to request the book?
Structure and mechanism of human diacylglycerol O-acyltransferase 1
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structure and mechanism of human diacylglycerol O-acyltransferase 1
2020
Overview
Diacylglycerol
O
-acyltransferase 1 (DGAT1) synthesizes triacylglycerides and is required for dietary fat absorption and fat storage in humans
1
. DGAT1 belongs to the membrane-bound
O
-acyltransferase (MBOAT) superfamily, members of which are found in all kingdoms of life and are involved in the acylation of lipids and proteins
2
,
3
. How human DGAT1 and other mammalian members of the MBOAT family recognize their substrates and catalyse their reactions is unknown. The absence of three-dimensional structures also hampers rational targeting of DGAT1 for therapeutic purposes. Here we present the cryo-electron microscopy structure of human DGAT1 in complex with an oleoyl-CoA substrate. Each DGAT1 protomer has nine transmembrane helices, eight of which form a conserved structural fold that we name the MBOAT fold. The MBOAT fold in DGAT1 forms a hollow chamber in the membrane that encloses highly conserved catalytic residues. The chamber has separate entrances for each of the two substrates, fatty acyl-CoA and diacylglycerol. DGAT1 can exist as either a homodimer or a homotetramer and the two forms have similar enzymatic activity. The N terminus of DGAT1 interacts with the neighbouring protomer and these interactions are required for enzymatic activity.
The structure of human diacylglycerol
O
-acyltransferase 1, a membrane protein that synthesizes triacylglycerides, is solved with cryo-electron microscopy, providing insight into its function and mechanism of enzymatic activity.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/80
/ 82/83
/ Acyl Coenzyme A - metabolism
/ Analysis
/ Diacylglycerol O-acyltransferase
/ Diacylglycerol O-Acyltransferase - chemistry
/ Diacylglycerol O-Acyltransferase - genetics
/ Diacylglycerol O-Acyltransferase - metabolism
/ Diacylglycerol O-Acyltransferase - ultrastructure
/ Enzymes
/ Helices
/ Humanities and Social Sciences
/ Humans
/ Lipids
/ Mammals
/ Proteins
/ Science
