1yon | pdb_00001yon

Escherichia coli ketopantoate reductase in complex with 2-monophosphoadenosine-5'-diphosphate

spinqualitylabelsall models 1yon, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1yon is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: A2R Related: 1ks9, 1yjq Gene: panE ("Bacillus coli" Migula 1895) Activity: 2-dehydropantoate 2-reductase, with EC number 1.1.1.169 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PANE_ECOLI] Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. 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 PubMed The crystal structure of Escherichia coli ketopantoate reductase in complex with 2'-monophosphoadenosine 5'-diphosphoribose, a fragment of NADP+ that lacks the nicotinamide ring, is reported. The ligand is bound at the enzyme active site in the opposite orientation to that observed for NADP+, with the adenine ring occupying the lipophilic nicotinamide pocket. Isothermal titration calorimetry with R31A and N98A mutants of the enzyme is used to show that the unusual ;reversed binding mode' observed in the crystal is triggered by changes in the protonation of binding groups at low pH. This research has important implications for fragment-based approaches to drug design, namely that the crystallization conditions and the chemical modification of ligands can have unexpected effects on the binding modes. pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study.,Ciulli A, Lobley CM, Tuck KL, Smith AG, Blundell TL, Abell C Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):171-8. Epub 2007, Jan 16. PMID:17242510 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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