1DVG

CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME; SELELENO-METHIONINE DERIVATIVE, MUTATED AT M51T,M93L,M155L,M191L.

1DVG の概要

• エントリーDOI: 10.2210/pdb1dvg/pdb
• 関連するPDBエントリー: 1DVE 1QQ8
• 分子名称: HEME OXYGENASE-1, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: all alpha, protein-substrate complex, oxidoreductase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Microsome: P06762
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62544.52

構造登録者

Sugishima, M.,Omata, Y.,Kakuta, Y.,Sakamoto, H.,Noguchi, M.,Fukuyama, K. (登録日: 2000-01-20, 公開日: 2000-04-12, 最終更新日: 2024-10-30)

主引用文献

Sugishima, M.,Omata, Y.,Kakuta, Y.,Sakamoto, H.,Noguchi, M.,Fukuyama, K.
Crystal structure of rat heme oxygenase-1 in complex with heme.
FEBS Lett., 471:61-66, 2000

PubMed Abstract: Heme oxygenase catalyzes the oxidative cleavage of protoheme to biliverdin, the first step of heme metabolism utilizing O(2) and NADPH. We determined the crystal structures of rat heme oxygenase-1 (HO-1)-heme and selenomethionyl HO-1-heme complexes. Heme is sandwiched between two helices with the delta-meso edge of the heme being exposed to the surface. Gly143N forms a hydrogen bond to the distal ligand of heme, OH(-). The distance between Gly143N and the ligand is shorter than that in the human HO-1-heme complex. This difference may be related to a pH-dependent change of the distal ligand of heme. Flexibility of the distal helix may control the stability of the coordination of the distal ligand to heme iron. The possible role of Gly143 in the heme oxygenase reaction is discussed.

PubMed: 10760513
DOI: 10.1016/S0014-5793(00)01353-3

実験手法

X-RAY DIFFRACTION (2.2 Å)