3oz7

Publication Abstract from PubMed

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 crystal forms, namely I222 and P6(1)22. I222 is solved using MAD and refined at 3A whereas P6(1)22A is solved using MR and refined at 2.7A. I222 has three monomers in asymmetric unit whereas P6(1)22 has two monomers in the asymmetric unit. Sulphate ion is located at the active site where ATP binds in both crystal forms, but no Mg(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(1)22 but only in A-chain of I222 crystal form.

Crystal structure of Plasmodium falciparum phosphoglycerate kinase: Evidence for anion binding in the basic patch.,Smith CD, Chattopadhyay D, Pal B Biochem Biophys Res Commun. 2011 Jul 25. PMID:21798238^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.