2ATF
X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056
Summary for 2ATF
| Entry DOI | 10.2210/pdb2atf/pdb |
| Descriptor | Cysteine dioxygenase type I, NICKEL (II) ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | mm.241056, pfam05995.2 cdo_i, bc013638, cupin family, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, oxidoreductase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 23276.22 |
| Authors | Wesenberg, G.E.,Phillips Jr., G.N.,Mccoy, J.G.,Bitto, E.,Bingman, C.A.,Allard, S.T.M.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2005-08-24, release date: 2005-10-18, Last modification date: 2024-10-30) |
| Primary citation | McCoy, J.G.,Bailey, L.J.,Bitto, E.,Bingman, C.A.,Aceti, D.J.,Fox, B.G.,Phillips, G.N. Structure and mechanism of mouse cysteine dioxygenase. Proc.Natl.Acad.Sci.Usa, 103:3084-3089, 2006 Cited by PubMed Abstract: Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Deficiencies in this enzyme have been linked to autoimmune diseases and neurological disorders. The x-ray crystal structure of CDO from Mus musculus was solved to a nominal resolution of 1.75 Angstroms. The sequence is 91% identical to that of a human homolog. The structure reveals that CDO adopts the typical beta-barrel fold of the cupin superfamily. The NE2 atoms of His-86, -88, and -140 provide the metal binding site. The structure further revealed a covalent linkage between the side chains of Cys-93 and Tyr-157, the cysteine of which is conserved only in eukaryotic proteins. Metal analysis showed that the recombinant enzyme contained a mixture of iron, nickel, and zinc, with increased iron content associated with increased catalytic activity. Details of the predicted active site are used to present and discuss a plausible mechanism of action for the enzyme. PubMed: 16492780DOI: 10.1073/pnas.0509262103 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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