Literature DB >> 28543853

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

Alfredo J Guerra1, Gustavo A Afanador1, Sean T Prigge1.   

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.
© 2017 Wiley Periodicals, Inc. © 2017 Wiley Periodicals, Inc.

Entities:  

Keywords:  LipL1; Plasmodium falciparum; lipoate; lipoate ligase; lipoylation; malaria

Mesh:

Substances:

Year:  2017        PMID: 28543853      PMCID: PMC5568926          DOI: 10.1002/prot.25324

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  35 in total

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