1vz5: Difference between revisions

Revision as of 16:38, 21 February 2008

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 as ligand. Known structural/functional Site: . 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

Page seeded by OCA on Thu Feb 21 15:38:55 2008

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 ==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, 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.
+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==
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 [[Category: Kertesz, M.]]
 [[Category: Mueller, I.]]
-[[Category: Stueckl, A.C.]]
+[[Category: Stueckl, A C.]]
 [[Category: Uson, I.]]
 [[Category: SIN]]
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 [[Category: sulfatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:17:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:38:55 2008''