7OZ1

Cryo-EM structure of ABCG1 E242Q mutant with ATP and cholesteryl hemisuccinate bound

7OZ1 の概要

• エントリーDOI: 10.2210/pdb7oz1/pdb
• EMDBエントリー: 13118
• 分子名称: Isoform 4 of ATP-binding cassette sub-family G member 1, ADENOSINE-5'-TRIPHOSPHATE, CHOLESTEROL HEMISUCCINATE, ... (4 entities in total)
• 機能のキーワード: cholesterol, abc transporter, atp binding, inward-open, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 157713.25

構造登録者

Skarda, L.,Kowal, J.,Locher, K.P. (登録日: 2021-06-25, 公開日: 2021-09-22, 最終更新日: 2021-09-29)

主引用文献

Skarda, L.,Kowal, J.,Locher, K.P.
Structure of the Human Cholesterol Transporter ABCG1.
J.Mol.Biol., 433:167218-167218, 2021

PubMed Abstract: ABCG1 is an ATP binding cassette (ABC) transporter that removes excess cholesterol from peripheral tissues. Despite its role in preventing lipid accumulation and the development of cardiovascular and metabolic disease, the mechanism underpinning ABCG1-mediated cholesterol transport is unknown. Here we report a cryo-EM structure of human ABCG1 at 4 Å resolution in an inward-open state, featuring sterol-like density in the binding cavity. Structural comparison with the multidrug transporter ABCG2 and the sterol transporter ABCG5/G8 reveals the basis of mechanistic differences and distinct substrate specificity. Benzamil and taurocholate inhibited the ATPase activity of liposome-reconstituted ABCG1, whereas the ABCG2 inhibitor Ko143 did not. Based on the structural insights into ABCG1, we propose a mechanism for ABCG1-mediated cholesterol transport.

PubMed: 34461069
DOI: 10.1016/j.jmb.2021.167218

実験手法

ELECTRON MICROSCOPY (4 Å)