1zxy
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Anthranilate Phosphoribosyltransferase from Sulfolobus solfataricus in complex with PRPP and Magnesium
OverviewOverview
The metabolic synthesis and degradation of essential nucleotide compounds, are primarily carried out by phosphoribosyltransferases (PRT) and, nucleoside phosphorylases (NP), respectively. Despite the resemblance of, their reactions, five classes of PRTs and NPs exist, where anthranilate, PRT (AnPRT) constitutes the only evolutionary link between synthesis and, degradation processes. We have characterized the active site of dimeric, AnPRT from Sulfolobus solfataricus by elucidating crystal structures of, the wild-type enzyme complexed to its two natural substrates anthranilate, and 5-phosphoribosyl-1-pyrophosphate/Mg(2+). These bind into two different, domains within each protomer and are brought together during catalysis by, rotational domain motions as shown by small angle x-ray scattering data., Steady-state kinetics of mutated AnPRT variants address the role of active, site residues in binding and catalysis. Results allow the comparative, analysis of PRT and pyrimidine NP families and expose related structural, motifs involved in nucleotide/nucleoside recognition by these enzyme, families.
About this StructureAbout this Structure
1ZXY is a Single protein structure of sequence from Sulfolobus solfataricus with MG and PRP as ligands. Active as Anthranilate phosphoribosyltransferase, with EC number 2.4.2.18 Full crystallographic information is available from OCA.
ReferenceReference
Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus., Marino M, Deuss M, Svergun DI, Konarev PV, Sterner R, Mayans O, J Biol Chem. 2006 Jul 28;281(30):21410-21. Epub 2006 May 19. PMID:16714288
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