2atf

File:2atf.gif

spinqualitylabelsall models 2atf, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056

OverviewOverview

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.

About this StructureAbout this Structure

2ATF is a Single protein structure of sequence from Mus musculus with NI and EDO as ligands. Active as Cysteine dioxygenase, with EC number 1.13.11.20 Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of mouse cysteine dioxygenase., McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr, Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3084-9. Epub 2006 Feb 21. PMID:16492780

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