2QPP

Crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme

2QPP の概要

• エントリーDOI: 10.2210/pdb2qpp/pdb
• 関連するPDBエントリー: 2Q32
• 分子名称: Heme oxygenase 2, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: ho-2, heme oxygenase, structural genomics medical relevance, structural genomics community request, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, endoplasmic reticulum, iron, metal-binding, microsome, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Microsome: P30519
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62215.52

構造登録者

Bianchetti, C.M.,Bingman, C.A.,Bitto, E.,Wesenberg, G.E.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (登録日: 2007-07-24, 公開日: 2007-08-07, 最終更新日: 2023-08-30)

主引用文献

Bianchetti, C.M.,Yi, L.,Ragsdale, S.W.,Phillips Jr., G.N.
Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2.
J.Biol.Chem., 282:37624-37631, 2007

PubMed Abstract: Heme oxygenase (HO) catalyzes the first step in the heme degradation pathway. The crystal structures of apo- and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs. Proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His(45), resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr(154), Lys(199), and Arg(203) orient the heme through direct interactions with the heme propionates. The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions.

PubMed: 17965015
DOI: 10.1074/jbc.M707396200

実験手法

X-RAY DIFFRACTION (2.61 Å)