6IVA

Crystal structure of the S. typhimurium oxaloacetate decarboxylase beta-gamma sub-complex

6IVA の概要

• エントリーDOI: 10.2210/pdb6iva/pdb
• 分子名称: Oxaloacetate decarboxylase beta chain, Probable oxaloacetate decarboxylase gamma chain (2 entities in total)
• 機能のキーワード: membrane protein, decarboxylase sodium pump, biotin-dependent decarboxylase
• 由来する生物種: Salmonella enterica I; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 168197.49

構造登録者

Xu, X.,Xiang, S. (登録日: 2018-12-03, 公開日: 2020-06-24, 最終更新日: 2023-11-22)

主引用文献

Xu, X.,Shi, H.,Gong, X.,Chen, P.,Gao, Y.,Zhang, X.,Xiang, S.
Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump.
Elife, 9:-, 2020

PubMed Abstract: The oxaloacetate decarboxylase sodium pump (OAD) is a unique primary-active transporter that utilizes the free energy derived from oxaloacetate decarboxylation for sodium transport across the cell membrane. It is composed of 3 subunits: the α subunit catalyzes carboxyl-transfer from oxaloacetate to biotin, the membrane integrated β subunit catalyzes the subsequent carboxyl-biotin decarboxylation and the coupled sodium transport, the γ subunit interacts with the α and β subunits and stabilizes the OAD complex. We present here structure of the OAD βγ sub-complex. The structure revealed that the β and γ subunits form a βγ hetero-hexamer with extensive interactions between the subunits and shed light on the OAD holo-enzyme assembly. Structure-guided functional studies provided insights into the sodium binding sites in the β subunit and the coupling between carboxyl-biotin decarboxylation and sodium transport by the OAD β subunit.

PubMed: 32459174
DOI: 10.7554/eLife.53853

実験手法

X-RAY DIFFRACTION (4.403 Å)