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Crystal structure of lipoate‐bound lipoate ligase 1, LipL1, from Plasmodium falciparum
Author(s) -
Guerra Alfredo J.,
Afanador Gustavo A.,
Prigge Sean T.
Publication year - 2017
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25324
Subject(s) - dna ligase , plasmodium falciparum , biology , computational biology , biochemistry , malaria , enzyme , immunology
Plasmodium falciparum lipoate protein ligase 1 ( Pf LipL1) is an ATP‐dependent ligase that belongs to the biotin/lipoate A/B protein ligase family (PFAM PF03099). Pf LipL1 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 Pf LipL1 (PfLipL1 Δ243‐279 ) 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.