ArticleThe Journal of biological chemistry2011
Crystal structure of Toxoplasma gondii porphobilinogen synthase: insights on octameric structure and porphobilinogen formation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Is heme metabolism a promising drug target in Toxoplasma gondii?PLoS pathogens · 2026Article
- Biochemical and molecular characterization of a novel porphobilinogen synthase from Corynebacterium glutamicum.World journal of microbiology & biotechnology · 2023Article
- The SeComputational toxicology (Amsterdam, Netherlands) · 2020Article
- Toxoplasma gondii requires its plant-like heme biosynthesis pathway for infection.PLoS pathogens · 2020Article
- Vitamin and cofactor acquisition in apicomplexans: SynthesisThe Journal of biological chemistry · 2020Review
- Wrangling Shape-Shifting Morpheeins to Tackle Disease and Approach Drug Discovery.Frontiers in molecular biosciences · 2020Review
- The Remarkable Character of Porphobilinogen Synthase.Accounts of chemical research · 2016Article
- wALADin benzimidazoles differentially modulate the function of porphobilinogen synthase orthologs.Journal of medicinal chemistry · 2014Article
- Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function.Current chemical biology · 2013Article
- Dynamic dissociating homo-oligomers and the control of protein function.Archives of biochemistry and biophysics · 2012Review
- Allostery and the dynamic oligomerization of porphobilinogen synthase.Archives of biochemistry and biophysics · 2012Review
- The search for the missing link: a relic plastid in Perkinsus?International journal for parasitology · 2011Review
- Structural genomics of infectious disease drug targets: the SSGCID.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Porphobilinogen synthase (PBGS) is essential for heme biosynthesis, but the enzyme of the protozoan parasite Toxoplasma gondii (TgPBGS) differs from that of its human host in several important respects, including subcellular localization, metal ion dependence, and quaternary structural dynamics. We have solved the crystal structure of TgPBGS, which contains an octamer in the crystallographic asymmetric unit. Crystallized in the presence of substrate, each active site contains one molecule of the product porphobilinogen. Unlike prior structures containing a substrate-derived heterocycle directly bound to an active site zinc ion, the product-bound TgPBGS active site contains neither zinc nor magnesium, placing in question the common notion that all PBGS enzymes require an active site metal ion. Unlike human PBGS, the TgPBGS octamer contains magnesium ions at the intersections between pro-octamer dimers, which are presumed to function in allosteric regulation. TgPBGS includes N- and C-terminal regions that differ considerably from previously solved crystal structures. In particular, the C-terminal extension found in all apicomplexan PBGS enzymes forms an intersubunit β-sheet, stabilizing a pro-octamer dimer and preventing formation of hexamers that can form in human PBGS. The TgPBGS structure suggests strategies for the development of parasite-selective PBGS inhibitors.
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