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Title: Crystal structure of Plasmodium falciparum phosphoglycerate kinase: Evidence for anion binding in the basic patch

Abstract

3-Phosphoglycerate kinase (EC 2.7.2.3) is a key enzyme in the glycolytic pathway and catalyzes an important phosphorylation step leading to the production of ATP. The crystal structure of Plasmodium falciparum phosphoglycerate kinase (PfPGK) in the open conformation is presented in two different groups, namely I222 and P6{sub 1}22. The structure in I222 space group is solved using MAD and refined at 3 {angstrom} whereas that in P6{sub 1}22A is solved using MR and refined at 2.7 {angstrom}. I222 form has three monomers in asymmetric unit whereas P6{sub 1}22 form has two monomers in the asymmetric unit. In both crystal forms a sulphate ion is located at the active site where ATP binds, but no Mg{sup 2+} ion is observed. For the first time another sulphate ion is found at the basic patch where the 3-phosphate of 1,3-biphosphoglycerate normally binds. This was found in both chains of P6{sub 1}22 form but only in chain A of I222 form.

Authors:
; ;  [1]
  1. (UAB)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
U.S. ARMY RESEARCH
OSTI Identifier:
1025645
Resource Type:
Journal Article
Journal Name:
Biochem. Biophys. Res. Commun.
Additional Journal Information:
Journal Volume: 412; Journal Issue: (2) ; 08, 2011; Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; ANIONS; CHAINS; CRYSTAL STRUCTURE; ENZYMES; GLYCOLYSIS; MONOMERS; PHOSPHORYLATION; PHOSPHOTRANSFERASES; PLASMODIUM; PRODUCTION; SPACE GROUPS

Citation Formats

Smith, Craig D., Chattopadhyay, Debasish, and Pal, Biswajit. Crystal structure of Plasmodium falciparum phosphoglycerate kinase: Evidence for anion binding in the basic patch. United States: N. p., 2012. Web. doi:10.1016/j.bbrc.2011.07.045.
Smith, Craig D., Chattopadhyay, Debasish, & Pal, Biswajit. Crystal structure of Plasmodium falciparum phosphoglycerate kinase: Evidence for anion binding in the basic patch. United States. doi:10.1016/j.bbrc.2011.07.045.
Smith, Craig D., Chattopadhyay, Debasish, and Pal, Biswajit. Fri . "Crystal structure of Plasmodium falciparum phosphoglycerate kinase: Evidence for anion binding in the basic patch". United States. doi:10.1016/j.bbrc.2011.07.045.
@article{osti_1025645,
title = {Crystal structure of Plasmodium falciparum phosphoglycerate kinase: Evidence for anion binding in the basic patch},
author = {Smith, Craig D. and Chattopadhyay, Debasish and Pal, Biswajit},
abstractNote = {3-Phosphoglycerate kinase (EC 2.7.2.3) is a key enzyme in the glycolytic pathway and catalyzes an important phosphorylation step leading to the production of ATP. The crystal structure of Plasmodium falciparum phosphoglycerate kinase (PfPGK) in the open conformation is presented in two different groups, namely I222 and P6{sub 1}22. The structure in I222 space group is solved using MAD and refined at 3 {angstrom} whereas that in P6{sub 1}22A is solved using MR and refined at 2.7 {angstrom}. I222 form has three monomers in asymmetric unit whereas P6{sub 1}22 form has two monomers in the asymmetric unit. In both crystal forms a sulphate ion is located at the active site where ATP binds, but no Mg{sup 2+} ion is observed. For the first time another sulphate ion is found at the basic patch where the 3-phosphate of 1,3-biphosphoglycerate normally binds. This was found in both chains of P6{sub 1}22 form but only in chain A of I222 form.},
doi = {10.1016/j.bbrc.2011.07.045},
journal = {Biochem. Biophys. Res. Commun.},
issn = {0006-291X},
number = (2) ; 08, 2011,
volume = 412,
place = {United States},
year = {2012},
month = {11}
}