3qva | pdb_00003qva

Structure of Klebsiella pneumoniae 5-hydroxyisourate hydrolase

spinqualitylabelsall models 3qva, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qva is a 4 chain structure with sequence from Klebsiella pneumoniae subsp. pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Gene: HpxT, KPN78578_16360, KPN_01666 (Klebsiella pneumoniae subsp. pneumoniae) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The stereospecific oxidative degradation of uric acid to (S)-allantoin has recently been demonstrated to proceed via two unstable intermediates and requires three separate enzymatic reactions. The second step of this reaction, the conversion of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline, is catalyzed by HIU hydrolase (HIUH). The high-resolution crystal structure of HIUH from the opportunistic pathogen Klebsiella pneumoniae (KpHIUH) has been determined. KpHIUH is a homotetrameric protein that, based on sequence and structural similarity, belongs to the transthyretin-related protein family. In addition, the steady-state kinetic parameters for this enzyme and four active-site mutants have been measured. These data provide valuable insight into the functional roles of the active-site residues. Based upon the structural and kinetic data, a mechanism is proposed for the KpHIUH-catalyzed reaction. Structural and kinetic insights into the mechanism of 5-hydroxyisourate hydrolase from Klebsiella pneumoniae.,French JB, Ealick SE Acta Crystallogr D Biol Crystallogr. 2011 Aug;67(Pt 8):671-7. Epub 2011, Jul 12. PMID:21795808 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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