1jxh
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(New page: 200px<br /><applet load="1jxh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jxh, resolution 2.3Å" /> '''4-Amino-5-hydroxymeth...)
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Revision as of 16:32, 20 November 2007
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4-Amino-5-hydroxymethyl-2-methylpyrimidine Phosphate Kinase from Salmonella typhimurium
Overview
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.
About this Structure
1JXH is a Single protein structure of sequence from Salmonella typhimurium with SO4 as ligand. Active as Phosphomethylpyrimidine kinase, with EC number 2.7.4.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase from Salmonella typhimurium at 2.3 A resolution., Cheng G, Bennett EM, Begley TP, Ealick SE, Structure. 2002 Feb;10(2):225-35. PMID:11839308
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