Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum

Alfredo J. Guerra, Gustavo A. Afanador, Sean T. Prigge

Research output: Contribution to journalArticlepeer-review

Abstract

Plasmodium falciparum lipoate protein ligase 1 (PfLipL1) is an ATP-dependent ligase that belongs to the biotin/lipoate A/B protein ligase family (PFAM PF03099). PfLipL1 is the only known canonical lipoate ligase in Pf and functions as a redox switch between two lipoylation routes in the parasite mitochondrion. Here, we report the crystal structure of a deletion construct of PfLipL1 (PfLipL1Δ243-279) bound to lipoate, and validate the lipoylation activity of this construct in both an in vitro lipoylation assay and a cell-based lipoylation assay. This characterization represents the first step in understanding the redox dependence of the lipoylation mechanism in malaria parasites. Proteins 2017; 85:1777–1783.

Original languageEnglish (US)
Pages (from-to)1777-1783
Number of pages7
JournalProteins: Structure, Function and Bioinformatics
Volume85
Issue number9
DOIs
StatePublished - Sep 2017

Keywords

  • LipL1
  • Plasmodium falciparum
  • lipoate
  • lipoate ligase
  • lipoylation
  • malaria

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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