ArticleProtein science : a publication of the Protein Society2012
Structural analysis of a 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with an N-terminal chorismate mutase-like regulatory domain.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 36 citations in OpenAlex.
- Bidirectional interdomain crosstalk in aFrontiers in microbiology · 2025Article
- A secreted form of chorismate mutase (Rv1885c) in Mycobacterium bovis BCG contributes to pathogenesis by inhibiting mitochondria-mediated apoptotic cell death of macrophages.Journal of biomedical science · 2023Article
- Influence of Cysteine 440 on the Active Site Properties of 3-Deoxy-d-Arabino-Heptulosonate 7-Phosphate Synthase inACS omega · 2023Article
- Biotechnological Advances in Resveratrol Production and its Chemical Diversity.Molecules (Basel, Switzerland) · 2019Review
- Domain cross-talk within a bifunctional enzyme provides catalytic and allosteric functionality in the biosynthesis of aromatic amino acids.The Journal of biological chemistry · 2019Article
- Article
- Structural and functional characterisation of the entry point to pyocyanin biosynthesis inBioscience reports · 2018Article
- Heterologous production of resveratrol in bacterial hosts: current status and perspectives.World journal of microbiology & biotechnology · 2018Review
- Exploring modular allostery via interchangeable regulatory domains.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structure of Chorismate Mutase-like Domain of DAHPS from Bacillus subtilis Complexed with Novel Inhibitor Reveals Conformational Plasticity of Active Site.Scientific reports · 2017Article
- Interdomain Conformational Changes Provide Allosteric Regulation en Route to Chorismate.The Journal of biological chemistry · 2016Article
- Neisseria meningitidis expresses a single 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase that is inhibited primarily by phenylalanine.Protein science : a publication of the Protein Society · 2013Article
- The diversity of allosteric controls at the gateway to aromatic amino acid biosynthesis.Protein science : a publication of the Protein Society · 2013Review
- Engineering allosteric control to an unregulated enzyme by transfer of a regulatory domain.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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5 authors at 1 institution in 1 country.
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Abstract
3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHPS) catalyzes the first step in the biosynthesis of a number of aromatic metabolites. Likely because this reaction is situated at a pivotal biosynthetic gateway, several DAHPS classes distinguished by distinct mechanisms of allosteric regulation have independently evolved. One class of DAHPSs contains a regulatory domain with sequence homology to chorismate mutase-an enzyme further downstream of DAHPS that catalyzes the first committed step in tyrosine/phenylalanine biosynthesis-and is inhibited by chorismate mutase substrate (chorismate) and product (prephenate). Described in this work, structures of the Listeria monocytogenes chorismate/prephenate regulated DAHPS in complex with Mn(2+) and Mn(2+) + phosphoenolpyruvate reveal an unusual quaternary architecture: DAHPS domains assemble as a tetramer, from either side of which chorismate mutase-like (CML) regulatory domains asymmetrically emerge to form a pair of dimers. This domain organization suggests that chorismate/prephenate binding promotes a stable interaction between the discrete regulatory and catalytic domains and supports a mechanism of allosteric inhibition similar to tyrosine/phenylalanine control of a related DAHPS class. We argue that the structural similarity of chorismate mutase enzyme and CML regulatory domain provides a unique opportunity for the design of a multitarget antibacterial.
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