1JXI

4-Amino-5-hydroxymethyl-2-methylpyrimidine Phosphate Kinase from Salmonella typhimurium complexed with 4-Amino-5-hydroxymethyl-2-methylpyrimidine

1JXI の概要

• エントリーDOI: 10.2210/pdb1jxi/pdb
• 分子名称: PHOSPHOMETHYLPYRIMIDINE KINASE, SULFATE ION, 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE, ... (4 entities in total)
• 機能のキーワード: thid, ribokinase family, kinase, phosphorylation, transferase
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63207.46

構造登録者

Cheng, G.,Bennett, E.M.,Begley, T.P.,Ealick, S.E. (登録日: 2001-09-07, 公開日: 2002-02-27, 最終更新日: 2024-04-03)

主引用文献

Cheng, G.,Bennett, E.M.,Begley, T.P.,Ealick, S.E.
Crystal structure of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase from Salmonella typhimurium at 2.3 A resolution.
Structure, 10:225-235, 2002

PubMed Abstract: The crystal structures of Salmonella typhimurium 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase (HMPP kinase) and its complex with substrate HMP have been determined. HMPP kinase catalyzes two separate ATP-dependent phosphorylation reactions and is an essential enzyme in the thiamin biosynthetic pathway. HMPP kinase is a homodimer with one active site per monomer and is structurally homologous to members of the ribokinase family. A comparison of the structure of HMPP kinase with other members of the ribokinase family suggests an evolutionary progression. Modeling studies suggest that HMPP kinase catalyzes both of its phosphorylation reactions using in-line displacement mechanisms. We propose that the active site accommodates the two separate reactions by providing two different binding modes for the phosphate group of HMP phosphate.

PubMed: 11839308
DOI: 10.1016/S0969-2126(02)00708-6

実験手法

X-RAY DIFFRACTION (2.64 Å)