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

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

doi:10.1002/prot.25324

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

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

Bloomberg School of Public Health

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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 (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.

Original language	English (US)
Pages (from-to)	1777-1783
Number of pages	7
Journal	Proteins: Structure, Function and Bioinformatics
Volume	85
Issue number	9
DOIs	https://doi.org/10.1002/prot.25324
State	Published - Sep 2017

Keywords

LipL1
Plasmodium falciparum
lipoate
lipoate ligase
lipoylation
malaria

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/prot.25324

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

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.",

keywords = "LipL1, Plasmodium falciparum, lipoate, lipoate ligase, lipoylation, malaria",

author = "Guerra, {Alfredo J.} and Afanador, {Gustavo A.} and Prigge, {Sean T.}",

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AU - Guerra, Alfredo J.

AU - Afanador, Gustavo A.

AU - Prigge, Sean T.

PY - 2017/9

Y1 - 2017/9

N2 - 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.

AB - 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.

KW - LipL1

KW - Plasmodium falciparum

KW - lipoate

KW - lipoate ligase

KW - lipoylation

KW - malaria

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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