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 line below this paragraph, {{ABSTRACT_PUBMED_15542595}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15542595 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15542595}}
==About this Structure==
==About this Structure==
Line 31:
Line 35:
[[Category: Self hydroxylation]]
[[Category: Self hydroxylation]]
[[Category: Sulfatase]]
[[Category: Sulfatase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:56:29 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:57:40 2008''
Revision as of 03:57, 29 July 2008
This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.
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
