7JM7

Structure of human CLC-7/OSTM1 complex

7JM7 の概要

• エントリーDOI: 10.2210/pdb7jm7/pdb
• 関連するPDBエントリー: 7JM6
• EMDBエントリー: 22386 22389
• 分子名称: Osteopetrosis-associated transmembrane protein 1, H(+)/Cl(-) exchange transporter 7, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: lysosomal, chloride-proton antiporter, chloride transport, ion transport, proton transport, complex, glycosylated, membrane protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 260082.77

構造登録者

Schrecker, M.,Hite, R. (登録日: 2020-07-31, 公開日: 2020-09-02, 最終更新日: 2024-10-16)

主引用文献

Schrecker, M.,Korobenko, J.,Hite, R.K.
Cryo-EM structure of the lysosomal chloride-proton exchanger CLC-7 in complex with OSTM1.
Elife, 9:-, 2020

PubMed Abstract: The chloride-proton exchanger CLC-7 plays critical roles in lysosomal homeostasis and bone regeneration and its mutation can lead to osteopetrosis, lysosomal storage disease and neurological disorders. In lysosomes and the ruffled border of osteoclasts, CLC-7 requires a β-subunit, OSTM1, for stability and activity. Here, we present electron cryomicroscopy structures of CLC-7 in occluded states by itself and in complex with OSTM1, determined at resolutions up to 2.8 Å. In the complex, the luminal surface of CLC-7 is entirely covered by a dimer of the heavily glycosylated and disulfide-bonded OSTM1, which serves to protect CLC-7 from the degradative environment of the lysosomal lumen. OSTM1 binding does not induce large-scale rearrangements of CLC-7, but does have minor effects on the conformation of the ion-conduction pathway, potentially contributing to its regulatory role. These studies provide insights into the role of OSTM1 and serve as a foundation for understanding the mechanisms of CLC-7 regulation.

PubMed: 32749217
DOI: 10.7554/eLife.59555

実験手法

ELECTRON MICROSCOPY (2.82 Å)