7V5D

Cryo-EM structure of the mouse ABCB9 (PG-bound)

7V5D の概要

• エントリーDOI: 10.2210/pdb7v5d/pdb
• EMDBエントリー: 31723
• 分子名称: ABC-type oligopeptide transporter ABCB9, (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE (2 entities in total)
• 機能のキーワード: abcb9, peptide transporter, lipid floppase, tapl, membrane protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 168844.63

構造登録者

Park, J.G.,Kim, S.,Jang, E.,Choi, S.H.,Han, H.,Ju, S.,Kim, J.W.,Min, D.S.,Jin, M.S. (登録日: 2021-08-17, 公開日: 2022-10-19, 最終更新日: 2024-06-12)

主引用文献

Park, J.G.,Kim, S.,Jang, E.,Choi, S.H.,Han, H.,Ju, S.,Kim, J.W.,Min, D.S.,Jin, M.S.
The lysosomal transporter TAPL has a dual role as peptide translocator and phosphatidylserine floppase.
Nat Commun, 13:5851-5851, 2022

PubMed Abstract: TAPL is a lysosomal ATP-binding cassette transporter that translocates a broad spectrum of polypeptides from the cytoplasm into the lysosomal lumen. Here we report that, in addition to its well-known role as a peptide translocator, TAPL exhibits an ATP-dependent phosphatidylserine floppase activity that is the possible cause of its high basal ATPase activity and of the lack of coupling between ATP hydrolysis and peptide efflux. We also present the cryo-EM structures of mouse TAPL complexed with (i) phospholipid, (ii) cholesteryl hemisuccinate (CHS) and 9-mer peptide, and (iii) ADP·BeF. The inward-facing structure reveals that F449 protrudes into the cylindrical transport pathway and divides it into a large hydrophilic central cavity and a sizable hydrophobic upper cavity. In the structure, the peptide binds to TAPL in horizontally-stretched fashion within the central cavity, while lipid molecules plug vertically into the upper cavity. Together, our results suggest that TAPL uses different mechanisms to function as a peptide translocase and a phosphatidylserine floppase.

PubMed: 36195619
DOI: 10.1038/s41467-022-33593-2

実験手法

ELECTRON MICROSCOPY (3.4 Å)