1JXH

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

Summary for 1JXH

• Entry DOI: 10.2210/pdb1jxh/pdb
• Related: 1JXI
• Descriptor: PHOSPHOMETHYLPYRIMIDINE KINASE, SULFATE ION (3 entities in total)
• Functional Keywords: thid, ribokinase family, phophorylation, kinase, transferase
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 2
• Total formula weight: 62929.15

Authors

Cheng, G.,Bennett, E.M.,Begley, T.P.,Ealick, S.E. (deposition date: 2001-09-07, release date: 2002-02-27, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)