3ETR
Crystal structure of xanthine oxidase in complex with lumazine
Summary for 3ETR
| Entry DOI | 10.2210/pdb3etr/pdb |
| Descriptor | Xanthine dehydrogenase/oxidase, FE2/S2 (INORGANIC) CLUSTER, FLAVIN-ADENINE DINUCLEOTIDE, ... (10 entities in total) |
| Functional Keywords | protein-ligand complex, enzyme catalysis, substrate orientation, fad, flavoprotein, iron, iron-sulfur, metal-binding, molybdenum, nad, oxidoreductase, peroxisome |
| Biological source | Bos taurus (Bovine) More |
| Cellular location | Cytoplasm : P80457 P80457 P80457 |
| Total number of polymer chains | 6 |
| Total formula weight | 273742.78 |
| Authors | Pauff, J.M.,Cao, H.,Hille, R. (deposition date: 2008-10-08, release date: 2009-01-27, Last modification date: 2023-09-06) |
| Primary citation | Pauff, J.M.,Cao, H.,Hille, R. Substrate Orientation and Catalysis at the Molybdenum Site in Xanthine Oxidase: CRYSTAL STRUCTURES IN COMPLEX WITH XANTHINE AND LUMAZINE. J.Biol.Chem., 284:8760-8767, 2009 Cited by PubMed Abstract: Xanthine oxidoreductase is a ubiquitous cytoplasmic protein that catalyzes the final two steps in purine catabolism. We have previously investigated the catalytic mechanism of the enzyme by rapid reaction kinetics and x-ray crystallography using the poor substrate 2-hydroxy-6-methylpurine, focusing our attention on the orientation of substrate in the active site and the role of Arg-880 in catalysis. Here we report additional crystal structures of as-isolated, functional xanthine oxidase in the course of reaction with the pterin substrate lumazine at 2.2 A resolution and of the nonfunctional desulfo form of the enzyme in complex with xanthine at 2.6 A resolution. In both cases the orientation of substrate is such that the pyrimidine subnucleus is oriented opposite to that seen with the slow substrate 2-hydroxy-6-methylpurine. The mechanistic implications as to how the ensemble of active site functional groups in the active site work to accelerate reaction rate are discussed. PubMed: 19109252DOI: 10.1074/jbc.M804517200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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