1A3A

CRYSTAL STRUCTURE OF IIA MANNITOL FROM ESCHERICHIA COLI

1A3A の概要

• エントリーDOI: 10.2210/pdb1a3a/pdb
• 分子名称: MANNITOL-SPECIFIC EII (2 entities in total)
• 機能のキーワード: phosphoenolpyruvate dependent phosphotransferase system, iia enzymes, histidine phosphorylation, phosphotransferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P00550
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 65394.19

構造登録者

Van Montfort, R.L.M.,Pijning, T.,Kalk, K.H.,Hangyi, I.,Kouwijzer, M.L.C.E.,Robillard, G.T.,Dijkstra, B.W. (登録日: 1998-01-19, 公開日: 1998-08-12, 最終更新日: 2024-02-07)

主引用文献

van Montfort, R.L.,Pijning, T.,Kalk, K.H.,Hangyi, I.,Kouwijzer, M.L.,Robillard, G.T.,Dijkstra, B.W.
The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site.
Structure, 6:377-388, 1998

PubMed Abstract: The bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) catalyses the cellular uptake and subsequent phosphorylation of carbohydrates. Moreover, the PTS plays a crucial role in the global regulation of various metabolic pathways. The PTS consists of two general proteins, enzyme I and the histidine-containing protein (HPr), and the carbohydrate-specific enzyme II (EII). EIIs are usually composed of two cytoplasmic domains, IIA and IIB, and a transmembrane domain, IIC. The IIA domains catalyse the transfer of a phosphoryl group from HPr to IIB, which phosphorylates the transported carbohydrate. Knowledge of the structures of the IIA proteins may provide insight into the mechanisms by which the PTS couples phosphorylation reactions with carbohydrate specificity.

PubMed: 9551558
DOI: 10.1016/S0969-2126(98)00039-2

実験手法

X-RAY DIFFRACTION (1.8 Å)