5HFT
Crystal structure of HpxW
Summary for 5HFT
| Entry DOI | 10.2210/pdb5hft/pdb |
| Descriptor | Gamma-glutamyltranspeptidase (2 entities in total) |
| Functional Keywords | amidohydrolase, transferase |
| Biological source | Klebsiella pneumoniae subsp. pneumoniae More |
| Total number of polymer chains | 4 |
| Total formula weight | 116603.31 |
| Authors | Ealick, S.E.,Hicks, K.A. (deposition date: 2016-01-07, release date: 2016-06-29, Last modification date: 2024-03-06) |
| Primary citation | Hicks, K.A.,Ealick, S.E. Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol, 72:808-816, 2016 Cited by PubMed Abstract: HpxW from the ubiquitous pathogen Klebsiella pneumoniae is involved in a novel uric acid degradation pathway downstream from the formation of oxalurate. Specifically, HpxW is an oxamate amidohydrolase which catalyzes the conversion of oxamate to oxalate and is a member of the Ntn-hydrolase superfamily. HpxW is autoprocessed from an inactive precursor to form a heterodimer, resulting in a 35.5 kDa α subunit and a 20 kDa β subunit. Here, the structure of HpxW is presented and the substrate complex is modeled. In addition, the steady-state kinetics of this enzyme and two active-site variants were characterized. These structural and biochemical studies provide further insight into this class of enzymes and allow a mechanism for catalysis consistent with other members of the Ntn-hydrolase superfamily to be proposed. PubMed: 27303801DOI: 10.1107/S2059798316007099 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.646 Å) |
Structure validation
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