1VZ5

Succinate Complex of AtsK

1VZ5 の概要

• エントリーDOI: 10.2210/pdb1vz5/pdb
• 関連するPDBエントリー: 1OIH 1OII 1OIJ 1OIK 1VZ4
• 分子名称: PUTATIVE ALKYLSULFATASE ATSK, SUCCINIC ACID (3 entities in total)
• 機能のキーワード: non-heme fe(ii) alphaketoglutarate dependent dioxygenase, alkylsulfatase, jelly roll, oxidoreductase, sulfatase, self hydroxylation
• 由来する生物種: PSEUDOMONAS PUTIDA
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 133465.96

構造登録者

Mueller, I.,Stueckl, A.C.,Uson, I.,Kertesz, M. (登録日: 2004-05-14, 公開日: 2004-11-15, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.15 Å)