5T8U

Crystal structure of P. falciparum LipL1 in complex lipoate

Summary for 5T8U

• Entry DOI: 10.2210/pdb5t8u/pdb
• Descriptor: Lipoate-protein ligase 1, LIPOIC ACID (3 entities in total)
• Functional Keywords: lipoylation, ligase
• Biological source: Plasmodium falciparum
• Total number of polymer chains: 2
• Total formula weight: 84822.32

Authors

Guerra, A.J.,Afanador, G.A.,Prigge, S.T. (deposition date: 2016-09-08, release date: 2017-05-31, Last modification date: 2023-10-04)

Primary citation

Guerra, A.J.,Afanador, G.A.,Prigge, S.T.
Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum.
Proteins, 85:1777-1783, 2017

PubMed 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 ) 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.

PubMed: 28543853
DOI: 10.1002/prot.25324

Experimental method

X-RAY DIFFRACTION (2.324 Å)