Purification, crystallization and preliminary X-ray diffraction analysis of pyridoxal kinase from Plasmodium falciparum (PfPdxK)

Author(s)

Kronenberger, Thales ; Lunev, Sergey ; Wrenger, Carsten ; Groves, Matthew R.

• Document type: Journal article
• Source: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS; v. 70, p. 6-pg., 2014-11-01.

Abstract

Pyridoxal kinases (PdxK) catalyze the phosphorylation of vitamin B-6 precursors. Thus, these enzymes are an essential part of many metabolic processes in all organisms. The protozoan parasite Plasmodium falciparum (the main causative agent of Malaria tropica) possesses a unique de novo B-6-biosynthesis pathway in addition to a interconversion pathway based on the activity of plasmodial PdxK (PfPdxK). The role of PdxK in B-6 salvage has prompted previous authors to suggest PdxK as a promising target for structure-based antimalarial drug design. Here, the expression, purification, crystallization and preliminary X-ray diffraction analysis of PfPdxK are reported. PfPdxK crystals have been grown in space group P2(1), with unit-cell parameters a = 52.7, b = 62.0, c = 93.7 angstrom, beta = 95 degrees. A data set has been collected to 2 angstrom resolution and an initial molecular-replacement solution is described. (AU)

• FAPESP's process: 13/10288-1 - Analysis of the organelle biogenesis in Plasmodium falciparum by live cell imaging
• Grantee: Carsten Wrenger
• Support Opportunities: Regular Research Grants
• FAPESP's process: 09/54325-2 - Elucidation of vitamin B metabolism in the human malaria parasite Plasmodium falciparum and their validation as a target for chemotherapy
• Grantee: Carsten Wrenger
• Support Opportunities: Research Grants - Young Investigators Grants
• FAPESP's process: 11/13706-3 - Implications from pyridoxine kinase of Plasmodium falciparum and study if its spacer regions
• Grantee: Thales Kronenberger
• Support Opportunities: Scholarships in Brazil - Master