Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly.

Abstract:

:The biochemical pathways involved in nicotinamide adenine dinucleotide (NAD) biosynthesis converge at the enzymatic step catalysed by nicotinamide mononucleotide adenylyltransferase (NMNAT, EC: 2.7.7.1). The majority of NMNATs are assembled into homo-oligomeric states that comprise 2-6 subunits. Recently, the NMNAT of Plasmodium falciparum (PfNMNAT) has been identified as a pharmacological target. The enzymatic characterisation, cellular location, and tertiary structure of the PfNMNAT protein have been reported. Nonetheless, its quaternary structure remains to be explored. The present study describes the oligomeric assembly of the 6 x His-PfNMNAT recombinant protein using immobilised metal affinity chromatography coupled with size exclusion chromatography (SEC) and native protein electrophoresis combined with Ferguson plot graphing. These chromatographic approaches resulted in the elution of an active monomer from the SEC column, whereas the Ferguson plot indicated a dimeric assembly of the 6 x His-PfNMNAT protein.

journal_name

Mem Inst Oswaldo Cruz

authors

Contreras-Rodríguez LE,Marin-Mogollon CY,Sánchez-Mejía LM,Ramírez-Hernández MH

doi

10.1590/0074-02760180073

subject

Has Abstract

pub_date

2018-07-10 00:00:00

pages

e180073

issue

9

eissn

0074-0276

issn

1678-8060

pii

S0074-02762018000900301

journal_volume

113

pub_type

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