2Y33

S-nitrosylated PHD2 (GSNO soaked) in complex with Zn(II) and UN9

2Y33 の概要

• エントリーDOI: 10.2210/pdb2y33/pdb
• 関連するPDBエントリー: 2G19 2G1M 2HBT 2HBU 2Y34
• 分子名称: EGL NINE HOMOLOG 1, ZINC ION, N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, non-heme, transcription and epigenetic regulation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28472.01

構造登録者

Chowdhury, R.,Clifton, I.J.,Schofield, C.J. (登録日: 2010-12-18, 公開日: 2010-12-29, 最終更新日: 2024-10-09)

主引用文献

Chowdhury, R.,Flashman, E.,Mecinovic, J.,Kramer, H.B.,Kessler, B.M.,Frapart, Y.M.,Boucher, J.-L.,Clifton, I.J.,McDonough, M.A.,Schofield, C.J.
Studies on the Reaction of Nitric Oxide with the Hypoxia-Inducible Factor Prolyl Hydroxylase Domain 2 (Egln1)
J.Mol.Biol., 410:268-279, 2011

PubMed Abstract: The hypoxic response in animals is mediated via the transcription factor hypoxia-inducible factor (HIF). An oxygen-sensing component of the HIF system is provided by Fe(II) and 2-oxoglutarate-dependent oxygenases that catalyse the posttranslational hydroxylation of the HIF-α subunit. It is proposed that the activity of the HIF hydroxylases can be regulated by their reaction with nitric oxide. We describe biochemical and biophysical studies on the reaction of prolyl hydroxylase domain-containing enzyme (PHD) isoform 2 (EGLN1) with nitric oxide and a nitric oxide transfer reagent. The combined results reveal the potential for the catalytic domain of PHD2 to react with nitric oxide both at its Fe(II) and at cysteine residues. Although the biological significance is unclear, the results suggest that the reaction of PHD2 with nitric oxide has the potential to be complex and are consistent with proposals based on cellular studies that nitric oxide may regulate the hypoxic response by direct reaction with the HIF hydroxylases.

PubMed: 21601578
DOI: 10.1016/J.JMB.2011.04.075

実験手法

X-RAY DIFFRACTION (2 Å)