1j58
From Proteopedia
(New page: 200px<br /><applet load="1j58" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j58, resolution 1.75Å" /> '''Crystal Structure of...) |
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| - | [[Image:1j58.jpg|left|200px]]<br /><applet load="1j58" size=" | + | [[Image:1j58.jpg|left|200px]]<br /><applet load="1j58" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1j58, resolution 1.75Å" /> | caption="1j58, resolution 1.75Å" /> | ||
'''Crystal Structure of Oxalate Decarboxylase'''<br /> | '''Crystal Structure of Oxalate Decarboxylase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Oxalate decarboxylase is a manganese-dependent enzyme that catalyzes the | + | Oxalate decarboxylase is a manganese-dependent enzyme that catalyzes the conversion of oxalate to formate and carbon dioxide. We have determined the structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A resolution in the presence of formate. The structure reveals a hexamer with 32-point symmetry in which each monomer belongs to the cupin family of proteins. Oxalate decarboxylase is further classified as a bicupin because it contains two cupin folds, possibly resulting from gene duplication. Each oxalate decarboxylase cupin domain contains one manganese binding site. Each of the oxalate decarboxylase domains is structurally similar to oxalate oxidase, which catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide. Amino acid side chains in the two metal binding sites of oxalate decarboxylase and the metal binding site of oxalate oxidase are very similar. Four manganese binding residues (three histidines and one glutamate) are conserved as well as a number of hydrophobic residues. The most notable difference is the presence of Glu333 in the metal binding site of the second cupin domain of oxalate decarboxylase. We postulate that this domain is responsible for the decarboxylase activity and that Glu333 serves as a proton donor in the production of formate. Mutation of Glu333 to alanine reduces the catalytic activity by a factor of 25. The function of the other domain in oxalate decarboxylase is not yet known. |
==About this Structure== | ==About this Structure== | ||
| - | 1J58 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MN, MG and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1J58 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J58 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Anand, R.]] | [[Category: Anand, R.]] | ||
| - | [[Category: Begley, T | + | [[Category: Begley, T P.]] |
| - | [[Category: Dorrestein, P | + | [[Category: Dorrestein, P C.]] |
| - | [[Category: Ealick, S | + | [[Category: Ealick, S E.]] |
[[Category: Kinsland, C.]] | [[Category: Kinsland, C.]] | ||
[[Category: FMT]] | [[Category: FMT]] | ||
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[[Category: oxalate]] | [[Category: oxalate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:03 2008'' |
Revision as of 11:19, 21 February 2008
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Crystal Structure of Oxalate Decarboxylase
Overview
Oxalate decarboxylase is a manganese-dependent enzyme that catalyzes the conversion of oxalate to formate and carbon dioxide. We have determined the structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A resolution in the presence of formate. The structure reveals a hexamer with 32-point symmetry in which each monomer belongs to the cupin family of proteins. Oxalate decarboxylase is further classified as a bicupin because it contains two cupin folds, possibly resulting from gene duplication. Each oxalate decarboxylase cupin domain contains one manganese binding site. Each of the oxalate decarboxylase domains is structurally similar to oxalate oxidase, which catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide. Amino acid side chains in the two metal binding sites of oxalate decarboxylase and the metal binding site of oxalate oxidase are very similar. Four manganese binding residues (three histidines and one glutamate) are conserved as well as a number of hydrophobic residues. The most notable difference is the presence of Glu333 in the metal binding site of the second cupin domain of oxalate decarboxylase. We postulate that this domain is responsible for the decarboxylase activity and that Glu333 serves as a proton donor in the production of formate. Mutation of Glu333 to alanine reduces the catalytic activity by a factor of 25. The function of the other domain in oxalate decarboxylase is not yet known.
About this Structure
1J58 is a Single protein structure of sequence from Bacillus subtilis with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A resolution., Anand R, Dorrestein PC, Kinsland C, Begley TP, Ealick SE, Biochemistry. 2002 Jun 18;41(24):7659-69. PMID:12056897
Page seeded by OCA on Thu Feb 21 13:19:03 2008
Categories: Bacillus subtilis | Single protein | Anand, R. | Begley, T P. | Dorrestein, P C. | Ealick, S E. | Kinsland, C. | FMT | MG | MN | Cupin | Decarboxyklase | Formate | Manganese | Oxalate
