2atf: Difference between revisions

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[[Image:2atf.gif|left|200px]]
{{Seed}}
[[Image:2atf.png|left|200px]]


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{{STRUCTURE_2atf|  PDB=2atf  |  SCENE=  }}  
{{STRUCTURE_2atf|  PDB=2atf  |  SCENE=  }}  


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




==Overview==
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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 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.
The line below this paragraph, {{ABSTRACT_PUBMED_16492780}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16492780 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16492780}}


==About this Structure==
==About this Structure==
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[[Category: Psi]]
[[Category: Psi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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