3LGN

Crystal structure of IsdI in complex with heme

3LGN の概要

• エントリーDOI: 10.2210/pdb3lgn/pdb
• 関連するPDBエントリー: 3LGM
• 分子名称: Heme-degrading monooxygenase isdI, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (5 entities in total)
• 機能のキーワード: dimeric alpha+beta barrel, cytoplasm, heme, iron, metal-binding, monooxygenase, oxidoreductase
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Cytoplasm (By similarity): Q7A827
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27352.06

構造登録者

Ukpabi, G.N.,Murphy, M.E.P. (登録日: 2010-01-20, 公開日: 2010-03-09, 最終更新日: 2023-11-01)

主引用文献

Reniere, M.L.,Ukpabi, G.N.,Harry, S.R.,Stec, D.F.,Krull, R.,Wright, D.W.,Bachmann, B.O.,Murphy, M.E.P.,Skaar, E.P.
The IsdG-family of haem oxygenases degrades haem to a novel chromophore
Mol.Microbiol., 75:1529-1538, 2010

PubMed Abstract: Enzymatic haem catabolism by haem oxygenases is conserved from bacteria to humans and proceeds through a common mechanism leading to the formation of iron, carbon monoxide and biliverdin. The first members of a novel class of haem oxygenases were recently identified in Staphylococcus aureus (IsdG and IsdI) and were termed the IsdG-family of haem oxygenases. Enzymes of the IsdG-family form tertiary structures distinct from those of the canonical haem oxygenase family, suggesting that IsdG-family members degrade haem via a unique reaction mechanism. Herein we report that the IsdG-family of haem oxygenases degrade haem to the oxo-bilirubin chromophore staphylobilin. We also present the crystal structure of haem-bound IsdI in which haem ruffling and constrained binding of oxygen is consistent with cleavage of the porphyrin ring at the beta- or delta-meso carbons. Combined, these data establish that the IsdG-family of haem oxygenases degrades haem to a novel chromophore distinct from biliverdin.

PubMed: 20180905
DOI: 10.1111/j.1365-2958.2010.07076.x

実験手法

X-RAY DIFFRACTION (1.5 Å)