ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Structure of Leishmania major cysteine synthase.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Benzoic and salicylic acids inhibit β-substituted alanine synthase 4;1 in common bean.Plant physiology · 2025Article
- Cysteine synthase: multiple structures of a key enzyme in cysteine synthesis and a potential drug target for Chagas disease and leishmaniasis.Acta crystallographica. Section D, Structural biology · 2023Article
- Lupeol Acetate and α-Amyrin Terpenes Activity againstTropical medicine and infectious disease · 2023Article
- Discovery of novel fragments inhibiting O-acetylserine sulphhydrylase by combining scaffold hopping and ligand-based drug design.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- Article
- The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.Molecules (Basel, Switzerland) · 2016Review
- Upregulation of Cysteine Synthase and Cystathionine β-Synthase Contributes to Leishmania braziliensis Survival under Oxidative Stress.Antimicrobial agents and chemotherapy · 2015Article
- Recent developments in drug discovery for leishmaniasis and human African trypanosomiasis.Chemical reviews · 2014Review
- In-silico analyses of sesquiterpene-related compounds on selected Leishmania enzyme-based targets.Molecules (Basel, Switzerland) · 2014Article
- Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target.PloS one · 2013Article
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Authors and funding
6 authors at 5 institutions in 1 country.
Funding
Abstract
Cysteine biosynthesis is a potential target for drug development against parasitic Leishmania species; these protozoa are responsible for a range of serious diseases. To improve understanding of this aspect of Leishmania biology, a crystallographic and biochemical study of L. major cysteine synthase has been undertaken, seeking to understand its structure, enzyme activity and modes of inhibition. Active enzyme was purified, assayed and crystallized in an orthorhombic form with a dimer in the asymmetric unit. Diffraction data extending to 1.8 Å resolution were measured and the structure was solved by molecular replacement. A fragment of γ-poly-D-glutamic acid, a constituent of the crystallization mixture, was bound in the enzyme active site. Although a D-glutamate tetrapeptide had insignificant inhibitory activity, the enzyme was competitively inhibited (K(i) = 4 µM) by DYVI, a peptide based on the C-terminus of the partner serine acetyltransferase with which the enzyme forms a complex. The structure surprisingly revealed that the cofactor pyridoxal phosphate had been lost during crystallization.
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