Cordeiro A T, Godoi P H, Delboni L F, Oliva G, Thiemann O H
Laboratory of Protein Crystallography and Structural Biology, Physics Institute of São Carlos, University of São Paulo - USP, Av. Trabalhador Sãocarlense 400, PO Box 369, 13566-590 São Carlos - SP, Brazil.
Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):592-5. doi: 10.1107/s0907444901001238.
Phosphoglucose isomerase (PGI) is the second enzyme in the glycolytic pathway and catalyzes an aldose-ketose isomerization. Outside the cell, PGI has been found to function as both a cytokine and as a growth factor. The human pgi gene was cloned and the expressed enzyme was purified to homogeneity. Isomorphous crystals were obtained under two conditions and belong to the P2(1)2(1)2(1) space group, with unit-cell parameters a = 80.37, b = 107.54, c = 270.33 A. A 94.7% complete data set was obtained and processed to a limiting resolution of 2.6 A. The asymmetric unit contains two hPGI dimers according to density calculations, a self-rotation function map and molecular-replacement solution.
磷酸葡萄糖异构酶(PGI)是糖酵解途径中的第二种酶,催化醛糖-酮糖异构化反应。在细胞外,已发现PGI兼具细胞因子和生长因子的功能。克隆了人类pgi基因,并将表达的酶纯化至同质。在两种条件下获得了同晶型晶体,它们属于P2(1)2(1)2(1)空间群,晶胞参数为a = 80.37、b = 107.54、c = 270.33 Å。获得了一个94.7%完整的数据集,并处理至2.6 Å的极限分辨率。根据密度计算、自旋转函数图和分子置换解决方案,不对称单元包含两个hPGI二聚体。