1JQN

Crystal structure of E.coli phosphoenolpyruvate carboxylase in complex with Mn2+ and DCDP

1JQN の概要

• エントリーDOI: 10.2210/pdb1jqn/pdb
• 関連するPDBエントリー: 1FIY 1jqo
• 分子名称: phosphoenolpyruvate carboxylase, MANGANESE (II) ION, ASPARTIC ACID, ... (5 entities in total)
• 機能のキーワード: beta barrel, mn2+ and dcdp complex, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 99598.49

構造登録者

Matsumura, H.,Kai, Y. (登録日: 2001-08-07, 公開日: 2003-01-14, 最終更新日: 2024-03-13)

主引用文献

Matsumura, H.,Xie, Y.,Shirakata, S.,Inoue, T.,Yoshinaga, T.,Ueno, Y.,Izui, K.,Kai, Y.
Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases.
Structure, 10:1721-1730, 2002

PubMed Abstract: Phosphoenolpyruvate carboxylase (PEPC) catalyzes the first step in the fixation of atmospheric CO(2) during C(4) photosynthesis. The crystal structure of C(4) form maize PEPC (ZmPEPC), the first structure of the plant PEPCs, has been determined at 3.0 A resolution. The structure includes a sulfate ion at the plausible binding site of an allosteric activator, glucose 6-phosphate. The crystal structure of E. coli PEPC (EcPEPC) complexed with Mn(2+), phosphoenolpyruvate analog (3,3-dichloro-2-dihydroxyphosphinoylmethyl-2-propenoate), and an allosteric inhibitor, aspartate, has also been determined at 2.35 A resolution. Dynamic movements were found in the ZmPEPC structure, compared with the EcPEPC structure, around two loops near the active site. On the basis of these molecular structures, the mechanisms for the carboxylation reaction and for the allosteric regulation of PEPC are proposed.

PubMed: 12467579
DOI: 10.1016/S0969-2126(02)00913-9

実験手法

X-RAY DIFFRACTION (2.35 Å)