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1U0E

Crystal structure of mouse phosphoglucose isomerase

1U0E の概要
エントリーDOI10.2210/pdb1u0e/pdb
関連するPDBエントリー1U0F 1U0G
分子名称Glucose-6-phosphate isomerase, SULFATE ION, BETA-MERCAPTOETHANOL, ... (5 entities in total)
機能のキーワードaldose-ketose isomerase, dimer, isomerase
由来する生物種Mus musculus (house mouse)
細胞内の位置Cytoplasm: P06745
タンパク質・核酸の鎖数2
化学式量合計129285.15
構造登録者
Solomons, J.T.G.,Zimmerly, E.M.,Burns, S.,Krishnamurthy, N.,Swan, M.K.,Krings, S.,Muirhead, H.,Chirgwin, J.,Davies, C. (登録日: 2004-07-13, 公開日: 2004-11-02, 最終更新日: 2023-08-23)
主引用文献Graham Solomons, J.T.,Zimmerly, E.M.,Burns, S.,Krishnamurthy, N.,Swan, M.K.,Krings, S.,Muirhead, H.,Chirgwin, J.,Davies, C.
The crystal structure of mouse phosphoglucose isomerase at 1.6A resolution and its complex with glucose 6-phosphate reveals the catalytic mechanism of sugar ring opening.
J.Mol.Biol., 342:847-860, 2004
Cited by
PubMed Abstract: Phosphoglucose isomerase (PGI) is an enzyme of glycolysis that interconverts glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) but, outside the cell, is a multifunctional cytokine. High-resolution crystal structures of the enzyme from mouse have been determined in native form and in complex with the inhibitor erythrose 4-phosphate, and with the substrate glucose 6-phosphate. In the substrate-bound structure, the glucose sugar is observed in both straight-chain and ring forms. This structure supports a specific role for Lys518 in enzyme-catalyzed ring opening and we present a "push-pull" mechanism in which His388 breaks the O5-C1 bond by donating a proton to the ring oxygen atom and, simultaneously, Lys518 abstracts a proton from the C1 hydroxyl group. The reverse occurs in ring closure. The transition from ring form to straight-chain substrate is achieved through rotation of the C3-C4 bond, which brings the C1-C2 region into close proximity to Glu357, the base catalyst for the isomerization step. The structure with G6P also explains the specificity of PGI for glucose 6-phosphate over mannose 6-isomerase (M6P). To isomerize M6P to F6P requires a rotation of its C2-C3 bond but in PGI this is sterically blocked by Gln511.
PubMed: 15342241
DOI: 10.1016/j.jmb.2004.07.085
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 1u0e
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2025-12-31に公開中

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