2gh2
From Proteopedia
(New page: 200px<br /><applet load="2gh2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gh2, resolution 1.500Å" /> '''1.5 A Resolution R....) |
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| - | [[Image:2gh2.gif|left|200px]]<br /><applet load="2gh2" size=" | + | [[Image:2gh2.gif|left|200px]]<br /><applet load="2gh2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2gh2, resolution 1.500Å" /> | caption="2gh2, resolution 1.500Å" /> | ||
'''1.5 A Resolution R. Norvegicus Cysteine Dioxygenase Structure Crystallized in the Presence of Cysteine'''<br /> | '''1.5 A Resolution R. Norvegicus Cysteine Dioxygenase Structure Crystallized in the Presence of Cysteine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cysteine dioxygenase is a mononuclear iron-dependent enzyme responsible | + | 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== | ==About this Structure== | ||
| - | 2GH2 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 SO4 and FE 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:// | + | 2GH2 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=SO4:'>SO4</scene> and <scene name='pdbligand=FE:'>FE</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=2GH2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Karplus, P | + | [[Category: Karplus, P A.]] |
| - | [[Category: Simmons, C | + | [[Category: Simmons, C R.]] |
| - | [[Category: Stipanuk, M | + | [[Category: Stipanuk, M H]] |
[[Category: FE]] | [[Category: FE]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: thioether]] | [[Category: thioether]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:35 2008'' |
Revision as of 15:31, 21 February 2008
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1.5 A Resolution R. Norvegicus Cysteine Dioxygenase Structure Crystallized in the Presence of Cysteine
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
2GH2 is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Active as Cysteine dioxygenase, with EC number 1.13.11.20 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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