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3S1I

Crystal structure of oxygen-bound hell's gate globin I

3S1I の概要
エントリーDOI10.2210/pdb3s1i/pdb
関連するPDBエントリー3S1J
分子名称Hemoglobin-like flavoprotein, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (5 entities in total)
機能のキーワードglobin, heme, oxygen-bound, autoxidation, oxygen transport, oxygen storage
由来する生物種Methylacidiphilum infernorum (METHYLOKORUS INFERNORUM)
タンパク質・核酸の鎖数3
化学式量合計50012.39
構造登録者
主引用文献Teh, A.H.,Saito, J.A.,Baharuddin, A.,Tuckerman, J.R.,Newhouse, J.S.,Kanbe, M.,Newhouse, E.I.,Rahim, R.A.,Favier, F.,Didierjean, C.,Sousa, E.H.S.,Stott, M.B.,Dunfield, P.F.,Gonzalez, G.,Gilles-Gonzalez, M.A.,Najimudin, N.,Alam, M.
Hell's Gate globin I: an acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin
Febs Lett., 585:3250-3258, 2011
Cited by
PubMed Abstract: Hell's Gate globin I (HGbI), a heme-containing protein structurally homologous to mammalian neuroglobins, has been identified from an acidophilic and thermophilic obligate methanotroph, Methylacidiphilum infernorum. HGbI has very high affinity for O(2) and shows barely detectable autoxidation in the pH range of 5.2-8.6 and temperature range of 25-50°C. Examination of the heme pocket by X-ray crystallography and molecular dynamics showed that conformational movements of Tyr29(B10) and Gln50(E7), as well as structural flexibility of the GH loop and H-helix, may play a role in modulating its ligand binding behavior. Bacterial HGbI's unique resistance to the sort of extreme acidity that would extract heme from any other hemoglobin makes it an ideal candidate for comparative structure-function studies of the expanding globin superfamily.
PubMed: 21925500
DOI: 10.1016/j.febslet.2011.09.002
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.77 Å)
構造検証レポート
Validation report summary of 3s1i
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-29に公開中

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