1IAT

CRYSTAL STRUCTURE OF HUMAN PHOSPHOGLUCOSE ISOMERASE/NEUROLEUKIN/AUTOCRINE MOTILITY FACTOR/MATURATION FACTOR

1IAT の概要

• エントリーDOI: 10.2210/pdb1iat/pdb
• 関連するPDBエントリー: 1DQR
• 分子名称: PHOSPHOGLUCOSE ISOMERASE, SULFATE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• 機能のキーワード: isomerase, glycolysis enzyme/neurotrophic growth factor/cytokine, two alpha/beta domains
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P06744
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 63369.00

構造登録者

Read, J.A.,Pearce, J.,Li, X.,Muirhead, H.,Chirgwin, J.,Davies, C. (登録日: 2001-03-23, 公開日: 2001-05-30, 最終更新日: 2024-04-03)

主引用文献

Read, J.,Pearce, J.,Li, X.,Muirhead, H.,Chirgwin, J.,Davies, C.
The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia.
J.Mol.Biol., 309:447-463, 2001

PubMed Abstract: Phosphoglucose isomerase (PGI) is a multifunctional protein, which, inside the cell, functions as a housekeeping enzyme of glycolysis and gluconeogenesis and, outside the cell, exerts wholly unrelated cytokine properties. We have determined the structure of human PGI to a resolution of 1.6 A using X-ray crystallography. The structure is highly similar to other PGIs, especially the architecture of the active site. Fortuitous binding of a sulphate molecule from the crystallisation solution has facilitated an accurate description of the substrate phosphate-binding site. Comparison with both native and inhibitor-bound rabbit PGI structures shows that two loops move closer to the active site upon binding inhibitor. Interestingly, the human structure most closely resembles the inhibitor-bound structure, suggesting that binding of the phosphate moiety of the substrate may trigger this conformational change. We suggest a new mechanism for catalysis that uses Glu357 as the base catalyst for the isomerase reaction rather than His388 as proposed previously. The human PGI structure has also provided a detailed framework with which to map mutations associated with non-spherocytic haemolytic anaemia.

PubMed: 11371164
DOI: 10.1006/jmbi.2001.4680

実験手法

X-RAY DIFFRACTION (1.62 Å)