3QVA
Structure of Klebsiella pneumoniae 5-hydroxyisourate hydrolase
Summary for 3QVA
| Entry DOI | 10.2210/pdb3qva/pdb |
| Descriptor | Transthyretin-like protein, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | transthyretin-related protein, 5-hydroxyisourate hydrolase, hydrolase |
| Biological source | Klebsiella pneumoniae subsp. pneumoniae |
| Total number of polymer chains | 4 |
| Total formula weight | 49957.18 |
| Authors | French, J.B.,Ealick, S.E. (deposition date: 2011-02-25, release date: 2011-08-24, Last modification date: 2024-02-21) |
| Primary citation | French, J.B.,Ealick, S.E. Structural and kinetic insights into the mechanism of 5-hydroxyisourate hydrolase from Klebsiella pneumoniae. Acta Crystallogr.,Sect.D, 67:671-677, 2011 Cited by PubMed Abstract: 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. PubMed: 21795808DOI: 10.1107/S090744491101746X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.755 Å) |
Structure validation
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