Crystal structure of human B-type phosphoglycerate mutase bound with citrate
Crystal structure of human B-type phosphoglycerate mutase bound with citrate
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DOI：
10.1016/j.bbrc.2005.03.243
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发表时间：
2005-06-17
影响因子：
3.1
通讯作者：
Gong, WM
中科院分区：
文献类型：
--
作者：
Wang, YL;Wei, ZY;Gong, WM
B型辅因子依赖性磷酸甘油酸酯酶（dPGM-B）以2，3-二磷酸甘油酸为辅因子，催化糖酵解和糖异生途径中2-磷酸甘油酸和3-磷酸甘油酸的相互转化。以两种晶型测定了与柠檬酸盐结合的人dPGM-B的晶体结构。这些结构揭示了dPGM和BPGM（二磷酸甘油酸变位酶）中保守的二聚化模式，并在此基础上提出了dPGM/BPGM异二聚体结构。结构比较支持残基13-21和98-117的构象变化决定PGM/BPGM活性差异。柠檬酸盐结合模式表明底物结合模式，与大肠杆菌dPGM/钒酸盐复合物的结构一致。在二聚体的中心发现了氯离子，为氯离子对dPGM活性的贡献提供了解释。基于结构信息，还讨论了在一些患者中发现的人dPGM突变缺陷的可能原因。(c)2005年爱思唯尔公司All rights reserved.
The B-type cofactor-dependent phosphoglycerate mutase (dPGM-B) catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in glycolysis and gluconeogenesis pathways using 2,3-bisphosphoglycerate as the cofactor. The crystal structures of human dPGM-B bound with citrate were determined in two crystal forms. These structures reveal a dimerization mode conserved in both of dPGM and BPGM (bisphosphoglycerate mutase), based on which a dPGM/BPGM heterodimer structure is proposed. Structural comparison supports that the conformational changes of residues 13-21 and 98-117 determine PGM/BPGM activity differences. The citrate-binding mode suggests a substrate-binding model, consistent with the structure of Escherichia coli dPGM/vanadate complex. A chloride ion was found in the center of the dimer, providing explanation for the contribution of chloride ion to dPGM activities. Based on the structural information, the possible reasons for the deficient human dPGM mutations found in some patients are also discussed. (c) 2005 Elsevier Inc. All rights reserved.