Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 9, Pages 3084-3089Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0509262103
Keywords
cupin; cysteine metabolism; O-2-activation
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Funding
- NCI NIH HHS [Y1-CO-1020] Funding Source: Medline
- NIGMS NIH HHS [P50 GM 64598, GM-50853, U54 GM074901, U54 GM 074901, P50 GM064598, Y1-GM-1104, R01 GM050853] Funding Source: Medline
- NLM NIH HHS [T15 LM007359] Funding Source: Medline
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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 angstrom. 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.
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