1VZ4

Fe-Succinate Complex of AtsK

Summary for 1VZ4

• Entry DOI: 10.2210/pdb1vz4/pdb
• Related: 1OIH 1OII 1OIJ 1OIK 1VZ5
• Descriptor: PUTATIVE ALKYLSULFATASE ATSK, FE (II) ION, SUCCINIC ACID, ... (4 entities in total)
• Functional Keywords: oxidoreductase, non-heme fe(ii) alphaketoglutarate dependent dioxygenase, alkylsulfatase, jelly roll, oxidoreductase sulfatase, self hydroxylation
• Biological source: PSEUDOMONAS PUTIDA
• Total number of polymer chains: 2
• Total formula weight: 66844.67

Authors

Mueller, I.,Stueckl, A.C.,Uson, I.,Kertesz, M. (deposition date: 2004-05-14, release date: 2004-11-15, Last modification date: 2023-12-13)

Primary citation

Mueller, I.,Stueckl, A.C.,Wakeley, J.,Kertesz, M.,Uson, I.
Succinate Complex Crystal Structures of the Alpha-Ketoglutarate-Dependent Dioxygenase Atsk: Steric Aspects of Enzyme Self-Hydroxylation
J.Biol.Chem., 280:5716-, 2005

PubMed Abstract: 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.

PubMed: 15542595
DOI: 10.1074/JBC.M410840200

Experimental method

X-RAY DIFFRACTION (2.5 Å)