ArticleActa crystallographica. Section F, Structural biology communications2019
Substrate-analogue complex structure of Mycobacterium tuberculosis decaprenyl diphosphate synthase.
Article in Acta crystallographica. Section F, Structural biology communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- Structural Prediction and Functional Mechanistic Characterization of Farnesyl Diphosphate Synthase fromACS omega · 2026Article
- Structural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex.Nature communications · 2020Article
- Structural elucidation of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Decaprenyl diphosphate synthase from Mycobacterium tuberculosis (MtDPPS, also known as Rv2361c) catalyzes the consecutive elongation of ω,E,Z-farnesyl diphosphate (EZ-FPP) by seven isoprene units by forming new cis double bonds. The protein folds into a butterfly-like homodimer like most other cis-type prenyltransferases. The starting allylic substrate EZ-FPP is bound to the S1 site and the homoallylic substrate to be incorporated, isopentenyl diphosphate, is bound to the S2 site. Here, a 1.55 Å resolution structure of MtDPPS in complex with the substrate analogues geranyl S-thiodiphosphate (GSPP) and isopentenyl S-thiodiphosphate bound to their respective sites in one subunit clearly shows the active-site configuration and the magnesium-coordinated geometry for catalysis. The ligand-binding mode of GSPP in the other subunit indicates a possible pathway of product translocation from the S2 site to the S1 site, as required for the next step of the reaction. The preferred binding of negatively charged effectors to the S1 site also suggests a promising direction for inhibitor design.
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