7ZZ8

Cryo-EM structure of Lactococcus lactis pyruvate carboxylase with acetyl-CoA and cyclic di-AMP

7ZZ8 の概要

• エントリーDOI: 10.2210/pdb7zz8/pdb
• EMDBエントリー: 15037
• 分子名称: Pyruvate carboxylase, MAGNESIUM ION, MANGANESE (II) ION, ... (8 entities in total)
• 機能のキーワード: tetramer, carboxylase, biotin, inhibitor, ligase
• 由来する生物種: Lactococcus lactis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 516428.66

構造登録者

Lopez-Alonso, J.P.,Lazaro, M.,Gil, D.,Choi, P.H.,Tong, L.,Valle, M. (登録日: 2022-05-25, 公開日: 2022-10-12, 最終更新日: 2023-11-15)

主引用文献

Lopez-Alonso, J.P.,Lazaro, M.,Gil-Carton, D.,Choi, P.H.,Tong, L.,Valle, M.
CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase.
Nat Commun, 13:6185-6185, 2022

PubMed Abstract: Pyruvate carboxylase (PC) is a tetrameric enzyme that contains two active sites per subunit that catalyze two consecutive reactions. A mobile domain with an attached prosthetic biotin links both reactions, an initial biotin carboxylation and the subsequent carboxyl transfer to pyruvate substrate to produce oxaloacetate. Reaction sites are at long distance, and there are several co-factors that play as allosteric regulators. Here, using cryoEM we explore the structure of active PC tetramers focusing on active sites and on the conformational space of the oligomers. The results capture the mobile domain at both active sites and expose catalytic steps of both reactions at high resolution, allowing the identification of substrates and products. The analysis of catalytically active PC tetramers reveals the role of certain motions during enzyme functioning, and the structural changes in the presence of additional cofactors expose the mechanism for allosteric regulation.

PubMed: 36261450
DOI: 10.1038/s41467-022-33987-2

実験手法

ELECTRON MICROSCOPY (3.29 Å)