2b5h

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[[Image:2b5h.gif|left|200px]]<br /><applet load="2b5h" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2b5h.gif|left|200px]]
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caption="2b5h, resolution 1.50&Aring;" />
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'''1.5 A Resolution Crystal Structure of Recombinant R. Norvegicus Cysteine Dioxygenase'''<br />
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{{Structure
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|PDB= 2b5h |SIZE=350|CAPTION= <scene name='initialview01'>2b5h</scene>, resolution 1.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</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=10116 Rattus norvegicus])
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}}
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'''1.5 A Resolution Crystal Structure of Recombinant R. Norvegicus Cysteine Dioxygenase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2B5H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2B5H OCA].
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2B5H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5H OCA].
==Reference==
==Reference==
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Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation., Simmons CR, Liu Q, Huang Q, Hao Q, Begley TP, Karplus PA, Stipanuk MH, J Biol Chem. 2006 Jul 7;281(27):18723-33. Epub 2006 Apr 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16611640 16611640]
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Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation., Simmons CR, Liu Q, Huang Q, Hao Q, Begley TP, Karplus PA, Stipanuk MH, J Biol Chem. 2006 Jul 7;281(27):18723-33. Epub 2006 Apr 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16611640 16611640]
[[Category: Cysteine dioxygenase]]
[[Category: Cysteine dioxygenase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: tetrahedral iron coordination]]
[[Category: tetrahedral iron coordination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:57:49 2008''

Revision as of 13:57, 20 March 2008


PDB ID 2b5h

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands:
Gene: Cdo1 (Rattus norvegicus)
Activity: Cysteine dioxygenase, with EC number 1.13.11.20
Coordinates: save as pdb, mmCIF, xml



1.5 A Resolution Crystal Structure of Recombinant R. Norvegicus Cysteine Dioxygenase


Overview

Cysteine dioxygenase is a mononuclear iron-dependent enzyme responsible for the oxidation of cysteine with molecular oxygen to form cysteine sulfinate. This reaction commits cysteine to either catabolism to sulfate and pyruvate or the taurine biosynthetic pathway. Cysteine dioxygenase is a member of the cupin superfamily of proteins. The crystal structure of recombinant rat cysteine dioxygenase has been determined to 1.5-A resolution, and these results confirm the canonical cupin beta-sandwich fold and the rare cysteinyltyrosine intramolecular cross-link (between Cys(93) and Tyr(157)) seen in the recently reported murine cysteine dioxygenase structure. In contrast to the catalytically inactive mononuclear Ni(II) metallocenter present in the murine structure, crystallization of a catalytically competent preparation of rat cysteine dioxygenase revealed a novel tetrahedrally coordinated mononuclear iron center involving three histidines (His(86), His(88), and His(140)) and a water molecule. Attempts to acquire a structure with bound ligand using either cocrystallization or soaking crystals with cysteine revealed the formation of a mixed disulfide involving Cys(164) near the active site, which may explain previously observed substrate inhibition. This work provides a framework for understanding the molecular mechanisms involved in thiol dioxygenation and sets the stage for exploration of the chemistry of both the novel mononuclear iron center and the catalytic role of the cysteinyl-tyrosine linkage.

About this Structure

2B5H is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation., Simmons CR, Liu Q, Huang Q, Hao Q, Begley TP, Karplus PA, Stipanuk MH, J Biol Chem. 2006 Jul 7;281(27):18723-33. Epub 2006 Apr 11. PMID:16611640

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