5t8u

Crystal structure of P. falciparum LipL1 in complex lipoate

spinqualitylabelsall models 5t8u, resolution 2.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5t8u is a 2 chain structure with sequence from Plasmodium falciparum 3D7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.324Å Ligands: LPA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LIPLA_PLAF7 Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes (PubMed:17244193, PubMed:25116855, PubMed:28543853). In the mitochondrion, functions as a redox switch between two lipoylation routes (PubMed:25116855). Senses the oxidation state of lipoate and determines which downstream enzymes will be lipoylated (PubMed:25116855). In low reducing conditions, uses lipoate in its oxidized ring form to lipoylate glycine cleavage system H-protein GCVH (PubMed:17244193, PubMed:25116855, PubMed:28543853). In high reducing conditions and together with LipL2, uses reduced lipoate (dihydrolipoate) to lipoylate the E2 component of the branched chain alpha-ketoacid dehydrogenase complex BCKDH-E2/BCDH and the E2 component of the alpha-ketoglutarate dehydrogenase complex KDH. LipL1 is responsible for catalysing the activation of lipoate, forming lipoyl-AMP while LipL2 is required but is not capable of catalyzing this reaction (PubMed:17244193, PubMed:25116855). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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