2ic1

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[[Image:2ic1.gif|left|200px]]<br /><applet load="2ic1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ic1.gif|left|200px]]
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caption="2ic1, resolution 2.7&Aring;" />
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'''Crystal Structure of Human Cysteine Dioxygenase in Complex with Substrate Cysteine'''<br />
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{{Structure
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|PDB= 2ic1 |SIZE=350|CAPTION= <scene name='initialview01'>2ic1</scene>, resolution 2.7&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> and <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cysteine_dioxygenase Cysteine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.20 1.13.11.20]
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|GENE= CDO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of Human Cysteine Dioxygenase in Complex with Substrate Cysteine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2IC1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FE2:'>FE2</scene> and <scene name='pdbligand=CYS:'>CYS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cysteine_dioxygenase Cysteine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.20 1.13.11.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IC1 OCA].
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2IC1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IC1 OCA].
==Reference==
==Reference==
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An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor., Ye S, Wu X, Wei L, Tang D, Sun P, Bartlam M, Rao Z, J Biol Chem. 2007 Feb 2;282(5):3391-402. Epub 2006 Nov 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17135237 17135237]
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An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor., Ye S, Wu X, Wei L, Tang D, Sun P, Bartlam M, Rao Z, J Biol Chem. 2007 Feb 2;282(5):3391-402. Epub 2006 Nov 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17135237 17135237]
[[Category: Cysteine dioxygenase]]
[[Category: Cysteine dioxygenase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: enzyme-substrate complex]]
[[Category: enzyme-substrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:27:42 2008''

Revision as of 15:27, 20 March 2008

Image:2ic1.gif


PDB ID 2ic1

Drag the structure with the mouse to rotate
, resolution 2.7Å
Ligands: and
Gene: CDO1 (Homo sapiens)
Activity: Cysteine dioxygenase, with EC number 1.13.11.20
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Human Cysteine Dioxygenase in Complex with Substrate Cysteine


Overview

Cysteine dioxygenase is a non-heme mononuclear iron metalloenzyme that catalyzes the oxidation of cysteine to cysteine sulfinic acid with addition of molecular dioxygen. This irreversible oxidative catabolism of cysteine initiates several important metabolic pathways related to diverse sulfurate compounds. Cysteine dioxygenase is therefore very important for maintaining the proper hepatic concentration of intracellular free cysteine. Mechanisms for mouse and rat cysteine dioxygenases have recently been reported based on their crystal structures in the absence of substrates, although there is still a lack of direct evidence. Here we report the first crystal structure of human cysteine dioxygenase in complex with its substrate L-cysteine to 2.7A, together with enzymatic activity and metal content assays of several single point mutants. Our results provide an insight into a new mechanism of cysteine thiol dioxygenation catalyzed by cysteine dioxygenase, which is tightly associated with a thioether-bonded tyrosine-cysteine cofactor involving Tyr-157 and Cys-93. This cross-linked protein-derived cofactor plays several key roles different from those in galactose oxidase. This report provides a new potential target for therapy of diseases related to human cysteine dioxygenase, including neurodegenerative and autoimmune diseases.

About this Structure

2IC1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor., Ye S, Wu X, Wei L, Tang D, Sun P, Bartlam M, Rao Z, J Biol Chem. 2007 Feb 2;282(5):3391-402. Epub 2006 Nov 29. PMID:17135237

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