2atf: Difference between revisions

Revision as of 09:53, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2atf.png

Template:STRUCTURE 2atf

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

Template:ABSTRACT PUBMED 16492780

About this StructureAbout this Structure

2ATF is a Single protein structure of sequence from Mus musculus. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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+===X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056===
-==Overview==
+<!--
-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.
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