Structural highlights
Publication Abstract from PubMed
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 (PfLipL1Delta243-279 ) 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. (c) 2017 Wiley Periodicals, Inc.
Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum.,Guerra AJ, Afanador GA, Prigge ST Proteins. 2017 May 24. doi: 10.1002/prot.25324. PMID:28543853[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guerra AJ, Afanador GA, Prigge ST. Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum. Proteins. 2017 May 24. doi: 10.1002/prot.25324. PMID:28543853 doi:http://dx.doi.org/10.1002/prot.25324
