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首页> 外文期刊>Journal of Molecular Biology >Conformational changes in phosphoglucose isomerase induced by ligand binding.
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Conformational changes in phosphoglucose isomerase induced by ligand binding.

机译：配体结合引起的磷酸葡萄糖异构酶的构象变化。

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摘要

Phosphoglucose isomerase (PGI; EC 5.3.1.9) is the second enzyme in glycolysis, where it catalyzes the isomerization of D-glucose-6-phosphate to D-fructose-6-phosphate. It is the same protein as autocrine motility factor, differentiation and maturation mediator, and neuroleukin. Here, we report a new X-ray crystal structure of rabbit PGI (rPGI) without ligands bound in its active site. The structure was solved at 1.8A resolution by isomorphous phasing with a previously solved X-ray crystal structure of the rPGI dimer containing 6-phosphogluconate in its active site. Comparison of the new structure to previously reported structures enables identification of conformational changes that occur during binding of substrate or inhibitor molecules. Ligand binding causes an induced fit of regions containing amino acid residues 209-215, 245-259 and 385-389. This conformational change differs from the change previously reported to occur between the ring-opening and isomerization steps, in which the helix containing residues 513-521 moves toward the bound substrate. Differences between the liganded and unliganded structures are limited to the region within and close to the active-site pocket.
机译：磷酸葡萄糖异构酶（PGI; EC 5.3.1.9）是糖酵解中的第二种酶，它催化D-葡萄糖-6-磷酸异构化为D-果糖-6-磷酸。它与自分泌运动因子，分化和成熟介质和神经白蛋白相同。在这里，我们报告了兔PGI（rPGI）的新X射线晶体结构，在其活性位点没有结合配体。通过以同构相定相，以先前解析的在其活性位点含有6-磷酸葡萄糖酸酯的rPGI二聚体的X射线晶体结构，以1.8A的分辨率解析了该结构。通过将新结构与先前报道的结构进行比较，可以鉴定在底物或抑制剂分子结合过程中发生的构象变化。配体结合引起包含氨基酸残基209-215、245-259和385-389的区域的诱导拟合。该构象变化不同于先前报道的在开环和异构化步骤之间发生的变化，在该变化中，含螺旋的残基513-521向结合的底物移动。配体和未配体结构之间的差异仅限于活性位点口袋内和附近的区域。

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