2atf

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|GENE= Cdo1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
|GENE= Cdo1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam05995 CDO_I]</span>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam05995 CDO_I]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2atf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2atf OCA], [http://www.ebi.ac.uk/pdbsum/2atf PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2atf RCSB]</span>
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2atf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2atf OCA], [http://www.ebi.ac.uk/pdbsum/2atf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2atf RCSB]</span>
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:21:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:57:04 2008''

Revision as of 22:57, 30 March 2008

Image:2atf.gif


PDB ID 2atf

Drag the structure with the mouse to rotate
, resolution 1.75Å
Ligands: , ,
Gene: Cdo1 (Mus musculus)
Activity: Cysteine dioxygenase, with EC number 1.13.11.20
Domains: CDO_I
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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.

About this Structure

2ATF is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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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