| First Author | McCoy JG | Year | 2006 |
| Journal | Proc Natl Acad Sci U S A | Volume | 103 |
| Issue | 9 | Pages | 3084-9 |
| PubMed ID | 16492780 | Mgi Jnum | J:107182 |
| Mgi Id | MGI:3620384 | Doi | 10.1073/pnas.0509262103 |
| Citation | McCoy JG, et al. (2006) Structure and mechanism of mouse cysteine dioxygenase. Proc Natl Acad Sci U S A 103(9):3084-9 |
| abstractText | 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. |
