1KBL

PYRUVATE PHOSPHATE DIKINASE

1KBL の概要

• エントリーDOI: 10.2210/pdb1kbl/pdb
• 関連するPDBエントリー: 1DIK
• 分子名称: PYRUVATE PHOSPHATE DIKINASE, AMMONIUM ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: transferase, phosphotransferase, kinase
• 由来する生物種: Clostridium symbiosum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 97138.50

構造登録者

Herzberg, O.,Chen, C.C.,Liu, S. (登録日: 2001-11-06, 公開日: 2002-01-30, 最終更新日: 2023-08-16)

主引用文献

Herzberg, O.,Chen, C.C.,Liu, S.,Tempczyk, A.,Howard, A.,Wei, M.,Ye, D.,Dunaway-Mariano, D.
Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis
Biochemistry, 41:780-787, 2002

PubMed Abstract: Crystals of pyruvate phosphate dikinase in complex with a substrate analogue inhibitor, phosphonopyruvate (K(i) = 3 microM), have been obtained in the presence of Mg(2+). The structure has been determined and refined at 2.2 A resolution, revealing that the Mg(2+)-bound phosphonopyruvate binds in the alpha/beta-barrel's central channel, at the C-termini of the beta-strands. The mode of binding resembles closely the previously proposed PEP substrate binding mode, inferred by the homology of the structure (but not sequence homology) to pyruvate kinase. Kinetic analysis of site-directed mutants, probing residues involved in inhibitor binding, showed that all mutations resulted in inactivation, confirming the key role that these residues play in catalysis. Comparison between the structure of the PPDK-phosphonopyruvate complex and the structures of two complexes of pyruvate kinase, one with Mg(2+)-bound phospholactate and the other with Mg(2+)-oxalate and ATP, revealed that the two enzymes share some key features that facilitate common modes of substrate binding. There are also important structural differences; most notably, the machinery for acid/base catalysis is different.

PubMed: 11790099
DOI: 10.1021/bi011799+

実験手法

X-RAY DIFFRACTION (1.94 Å)