1vz5: Difference between revisions
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==Overview== | ==Overview== | ||
The alkylsulfatase AtsK from Pseudomonas putida S-313 is a member of the, non-heme iron(II)-alpha-ketoglutarate-dependent dioxygenase superfamily., In the initial step of their catalytic cycle, enzymes belonging to this, widespread and versatile family coordinate molecular oxygen to the iron, center in the active site. The subsequent decarboxylation of the, cosubstrate alpha-ketoglutarate yields carbon dioxide, succinate, and a, highly reactive ferryl (IV) species, which is required for substrate, oxidation via a complex mechanism involving the transfer of radical, species. Non-productive activation of oxygen may lead to harmful side, reactions; therefore, such enzymes need an effective built-in protection, mechanism. One of the ways of controlling undesired side reactions is the, . | The alkylsulfatase AtsK from Pseudomonas putida S-313 is a member of the, non-heme iron(II)-alpha-ketoglutarate-dependent dioxygenase superfamily., In the initial step of their catalytic cycle, enzymes belonging to this, widespread and versatile family coordinate molecular oxygen to the iron, center in the active site. The subsequent decarboxylation of the, cosubstrate alpha-ketoglutarate yields carbon dioxide, succinate, and a, highly reactive ferryl (IV) species, which is required for substrate, oxidation via a complex mechanism involving the transfer of radical, species. Non-productive activation of oxygen may lead to harmful side, reactions; therefore, such enzymes need an effective built-in protection, mechanism. One of the ways of controlling undesired side reactions is the, self-hydroxylation of an aromatic side chain, which leads to an, irreversibly inactivated species. Here we describe the crystal structure, of the alkylsulfatase AtsK in complexes with succinate and with, Fe(II)/succinate. In the crystal structure of the AtsK-Fe(II)-succinate, complex, the side chain of Tyr(168) is co-ordinated to the iron, suggesting that Tyr(168) is the target of enzyme self-hydroxylation. This, is the first structural study of an Fe(II)-alpha-ketoglutarate-dependent, dioxygenase that presents an aromatic side chain coordinated to the metal, center, thus allowing structural insight into this protective mechanism of, enzyme self-inactivation. | ||
==About this Structure== | ==About this Structure== | ||
1VZ5 is a | 1VZ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with SIN as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZ5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: sulfatase]] | [[Category: sulfatase]] | ||
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Revision as of 16:14, 5 November 2007
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SUCCINATE COMPLEX OF ATSK
OverviewOverview
The alkylsulfatase AtsK from Pseudomonas putida S-313 is a member of the, non-heme iron(II)-alpha-ketoglutarate-dependent dioxygenase superfamily., In the initial step of their catalytic cycle, enzymes belonging to this, widespread and versatile family coordinate molecular oxygen to the iron, center in the active site. The subsequent decarboxylation of the, cosubstrate alpha-ketoglutarate yields carbon dioxide, succinate, and a, highly reactive ferryl (IV) species, which is required for substrate, oxidation via a complex mechanism involving the transfer of radical, species. Non-productive activation of oxygen may lead to harmful side, reactions; therefore, such enzymes need an effective built-in protection, mechanism. One of the ways of controlling undesired side reactions is the, self-hydroxylation of an aromatic side chain, which leads to an, irreversibly inactivated species. Here we describe the crystal structure, of the alkylsulfatase AtsK in complexes with succinate and with, Fe(II)/succinate. In the crystal structure of the AtsK-Fe(II)-succinate, complex, the side chain of Tyr(168) is co-ordinated to the iron, suggesting that Tyr(168) is the target of enzyme self-hydroxylation. This, is the first structural study of an Fe(II)-alpha-ketoglutarate-dependent, dioxygenase that presents an aromatic side chain coordinated to the metal, center, thus allowing structural insight into this protective mechanism of, enzyme self-inactivation.
About this StructureAbout this Structure
1VZ5 is a Single protein structure of sequence from Pseudomonas putida with SIN as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Succinate complex crystal structures of the alpha-ketoglutarate-dependent dioxygenase AtsK: steric aspects of enzyme self-hydroxylation., Muller I, Stuckl C, Wakeley J, Kertesz M, Uson I, J Biol Chem. 2005 Feb 18;280(7):5716-23. Epub 2004 Nov 12. PMID:15542595
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