1tz6
From Proteopedia
Crystal structure of aminoimidazole riboside kinase from Salmonella enterica complexed with aminoimidazole riboside and ATP analog
Structural highlights
FunctionAIRSK_SALTY Phosphorylates 5-amino-1-(beta-D-ribosyl)imidazole (AIRs) to form 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole (AIR), an important intermediate in the purine and thiamine biosynthetic pathways (PubMed:12486071). It allows the use of exogenous aminoimidazole riboside (AIRs) to satisfy the cellular requirement for purines and thiamine (PubMed:12486071).[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structures of a Salmonella enterica aminoimidazole riboside (AIRs) kinase, its complex with the substrate AIRs, and its complex with AIRs and an ATP analog were determined at 2.6 angstroms, 2.9 angstroms, and 2.7 angstroms, respectively. The product of the Salmonella-specific gene stm4066, AIRs kinase, is a homodimer with one active site per monomer. The core structure, consisting of an eight-stranded beta sheet flanked by eight alpha helices, indicates that AIRs kinase is a member of the ribokinase superfamily. Unlike ribokinase and adenosine kinase in this superfamily, AIRs kinase does not show significant conformational changes upon substrate binding. The active site is covered by a lid formed by residues 16-28 and 86-100. A comparison of the structure of AIRs kinase with other ribokinase superfamily members suggests that the active site lid and conformational changes that occur upon substrate binding may be advanced features in the evolution of the ribokinase superfamily. Crystal structure of an aminoimidazole riboside kinase from Salmonella enterica: implications for the evolution of the ribokinase superfamily.,Zhang Y, Dougherty M, Downs DM, Ealick SE Structure. 2004 Oct;12(10):1809-21. PMID:15458630[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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