ArticleThe Journal of biological chemistry2013
Crystal structure of Mycobacterium tuberculosis polyketide synthase 11 (PKS11) reveals intermediates in the synthesis of methyl-branched alkylpyrones.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Experimental, Genomic, and Structural Evidence Supporting Putative PET-Hydrolases in Thermophilic Bacteria Isolated From Hot Springs in Cajamarca, Peru.MicrobiologyOpen · 2026Article
- Contribution of Proteins to Membrane and Cell Wall Structures in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Article
- Structural insights into type III polyketide synthase CylI from cylindrocyclophane biosynthesis.Protein science : a publication of the Protein Society · 2024Article
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- InsPection of electron density maps supports wrongly modeled hexakisphosphate (InsP6) bound to African swine fever mRNA-decapping enzyme g5Rp.Journal of virology · 2024Article
- Identification of 1,3,6,8-Tetrahydroxynaphthalene Synthase (ThnA) fromJournal of microbiology and biotechnology · 2023Article
- Cloning and Molecular Characterization of theAntibiotics (Basel, Switzerland) · 2023Article
- A Type III Polyketide Synthase Specific for Sporulating Negativicutes is Responsible for Alkylpyrone Biosynthesis.Chembiochem : a European journal of chemical biology · 2022Article
- Synthetic approaches to potent heterocyclic inhibitors of tuberculosis: A decade review.Frontiers in pharmacology · 2022Review
- Function, essentiality, and expression of cytochrome P450 enzymes and their cognate redox partners in Mycobacterium tuberculosis: are they drug targets?Applied microbiology and biotechnology · 2019Review
- Genome mining reveals uncommon alkylpyrones as type III PKS products from myxobacteria.Journal of industrial microbiology & biotechnology · 2019Article
- Novel Type III Polyketide Synthases Biosynthesize Methylated Polyketides in Mycobacterium marinum.Scientific reports · 2018Article
- Synthesis andMedChemComm · 2018Article
- Exploiting the Biosynthetic Potential of Type III Polyketide Synthases.Molecules (Basel, Switzerland) · 2016Review
- Structural basis of head to head polyketide fusion by CorB.Chemical science · 2015Article
- Architecture of the polyketide synthase module: surprises from electron cryo-microscopy.Current opinion in structural biology · 2015Review
- Production of recombinant proteins in Mycobacterium smegmatis for structural and functional studies.Protein science : a publication of the Protein Society · 2015Review
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8 authors at 3 institutions in 1 country.
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Abstract
PKS11 is one of three type III polyketide synthases (PKSs) identified in Mycobacterium tuberculosis. Although many PKSs in M. tuberculosis have been implicated in producing complex cell wall glycolipids, the biological function of PKS11 is unknown. PKS11 has previously been proposed to synthesize alkylpyrones from fatty acid substrates. We solved the crystal structure of M. tuberculosis PKS11 and found the overall fold to be similar to other type III PKSs. PKS11 has a deep hydrophobic tunnel proximal to the active site Cys-138 to accommodate substrates. We observed electron density in this tunnel from a co-purified molecule that was identified by mass spectrometry to be palmitate. Co-crystallization with malonyl-CoA (MCoA) or methylmalonyl-CoA (MMCoA) led to partial turnover of the substrate, resulting in trapped intermediates. Reconstitution of the reaction in solution confirmed that both co-factors are required for optimal activity, and kinetic analysis shows that MMCoA is incorporated first, then MCoA, followed by lactonization to produce methyl-branched alkylpyrones.
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