3D8H

Crystal structure of phosphoglycerate mutase from Cryptosporidium parvum, cgd7_4270

3D8H の概要

• エントリーDOI: 10.2210/pdb3d8h/pdb
• 分子名称: Glycolytic phosphoglycerate mutase (2 entities in total)
• 機能のキーワード: structural genomics, malaria, cryptosporidium, glycolysis, isomerase, structural genomics consortium, sgc
• 由来する生物種: Cryptosporidium parvum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60411.41

構造登録者

Wernimont, A.K.,Lew, J.,Wasney, G.,Alam, Z.,Kozieradzki, I.,Cossar, D.,Schapiro, M.,Bochkarev, A.,Arrowsmith, C.H.,Bountra, C.,Wilkstrom, M.,Edwards, A.M.,Hui, R.,Artz, J.D.,Hills, T.,Structural Genomics Consortium (SGC) (登録日: 2008-05-23, 公開日: 2008-07-15, 最終更新日: 2023-08-30)

主引用文献

Hills, T.,Srivastava, A.,Ayi, K.,Wernimont, A.K.,Kain, K.,Waters, A.P.,Hui, R.,Pizarro, J.C.
Characterization of a new phosphatase from Plasmodium.
Mol.Biochem.Parasitol., 179:69-79, 2011

PubMed Abstract: Plasmodium falciparum malaria is the most important parasitic disease worldwide, responsible for an estimated 1 million deaths annually. Two P. falciparum genes code for putative phosphoglycerate mutases (PGMases), a widespread protein group characterized by the involvement of histidine residues in their catalytic mechanism. PGMases are responsible for the interconversion between 2 and 3-phosphoglycerate, an intermediate step in the glycolysis pathway. We have determined the crystal structures of one of the P. falciparum's PGMases (PfPGM2) and a functionally distinct phosphoglycerate mutase from Cryptosporidium parvum, a related apicomplexan parasite. We performed sequence and structural comparisons between the two structures, another P. falciparum enzyme (PfPGM1) and several other PGM family members from other organisms. The comparisons revealed a distinct conformation of the catalytically active residues not seen in previously determined phosphoglycerate mutase structures. Furthermore, characterization of their enzymatic activities revealed contrasting behaviors between the PfPGM2 and the classical cofactor-dependent PGMase from C. parvum, clearly establishing PfPGM2 as a phosphatase with a residual level of mutase activity. Further support for this function attribution was provided by our structural comparison with previously characterized PGM family members. Genetic characterization of PGM2 in the rodent parasite Plasmodium berghei indicated that the protein might be essential to blood stage asexual growth, and a GFP tagged allele is expressed in both blood and zygote ookinete development and located in the cytoplasm. The P. falciparum PGM2 is either an enzyme implicated in the phosphate metabolism of the parasite or a regulator of its life cycle.

PubMed: 21689687
DOI: 10.1016/j.molbiopara.2011.06.001

実験手法

X-RAY DIFFRACTION (2.01 Å)