1RFT

Crystal structure of pyridoxal kinase complexed with AMP-PCP and pyridoxamine

1RFT の概要

• エントリーDOI: 10.2210/pdb1rft/pdb
• 関連するPDBエントリー: 1LHP 1LHR 1RFU 1RFV
• 分子名称: Pyridoxal kinase, ZINC ION, POTASSIUM ION, ... (6 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Ovis aries (sheep)
• 細胞内の位置: Cytoplasm: P82197
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35638.79

構造登録者

Liang, D.-C.,Jiang, T.,Li, M.-H. (登録日: 2003-11-10, 公開日: 2004-04-27, 最終更新日: 2023-10-25)

主引用文献

Li, M.-H.,Kwok, F.,Chang, W.-R.,Liu, S.-Q.,Lo, S.C.L.,Zhang, J.-P.,Jiang, T.,Liang, D.-C.
Conformational changes in the reaction of pyridoxal kinase
J.BIOL.CHEM., 279:17459-17465, 2004

PubMed Abstract: To understand the processes involved in the catalytic mechanism of pyridoxal kinase (PLK),1 we determined the crystal structures of PLK.AMP-PCP-pyridoxamine, PLK.ADP.PLP, and PLK.ADP complexes. Comparisons of these structures have revealed that PLK exhibits different conformations during its catalytic process. After the binding of AMP-PCP (an analogue that replaced ATP) and pyridoxamine to PLK, this enzyme retains a conformation similar to that of the PLK.ATP complex. The distance between the reacting groups of the two substrates is 5.8 A apart, indicating that the position of ATP is not favorable to spontaneous transfer of its phosphate group. However, the structure of PLK.ADP.PLP complex exhibited significant changes in both the conformation of the enzyme and the location of the ligands at the active site. Therefore, it appears that after binding of both substrates, the enzyme-substrate complex requires changes in the protein structure to enable the transfer of the phosphate group from ATP to vitamin B(6). Furthermore, a conformation of the enzyme-substrate complex before the transition state of the enzymatic reaction was also hypothesized.

PubMed: 14722069
DOI: 10.1074/jbc.M312380200

実験手法

X-RAY DIFFRACTION (2.8 Å)