ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structure of NDP-forming Acetyl-CoA synthetase ACD1 reveals a large rearrangement for phosphoryl transfer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 35 citations in OpenAlex.
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- Therapeutic Targets and Approaches to Manage Inflammation of NAFLD.Biomedicines · 2025Review
- Crystal structure of the 4-hydroxybutyryl-CoA synthetase (ADP-forming) from nitrosopumilus maritimus.Communications biology · 2024Article
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- Rational Design of Daunorubicin C-14 Hydroxylase Based on the Understanding of Its Substrate-Binding Mechanism.International journal of molecular sciences · 2023Article
- Rapid Biocatalytic Synthesis of Aromatic Acid CoA Thioesters by Using Microbial Aromatic Acid CoA Ligases.Chembiochem : a European journal of chemical biology · 2023Article
- Applying biochemical and structural characterization of hydroxycinnamate catabolic enzymes from soil metagenome for lignin valorization strategies.Applied microbiology and biotechnology · 2022Article
- The many ways that nature has exploited the unusual structural and chemical properties of phosphohistidine for use in proteins.The Biochemical journal · 2021Review
- The biology of thermoacidophilic archaea from the order Sulfolobales.FEMS microbiology reviews · 2021Article
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- Glucose Metabolism and Acetate Switch in Archaea: the Enzymes in Haloferax volcanii.Journal of bacteriology · 2021Article
- Second distinct conformation of the phosphohistidine loop in succinyl-CoA synthetase.Acta crystallographica. Section D, Structural biology · 2021Article
- Tartryl-CoA inhibits succinyl-CoA synthetase.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Older Than Genes: The Acetyl CoA Pathway and Origins.Frontiers in microbiology · 2020Review
- Identification of the active site residues in ATP-citrate lyase's carboxy-terminal portion.Protein science : a publication of the Protein Society · 2019Article
- Sediment, methane and energy.Nature microbiology · 2019Article
- An alkaline active feruloyl-CoA synthetase from soil metagenome as a potential key enzyme for lignin valorization strategies.PloS one · 2019Article
- Structural intermediates and directionality of the swiveling motion of Pyruvate Phosphate Dikinase.Scientific reports · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NDP-forming acyl-CoA synthetases (ACDs) catalyze the conversion of various CoA thioesters to the corresponding acids, conserving their chemical energy in form of ATP. The ACDs are the major energy-conserving enzymes in sugar and peptide fermentation of hyperthermophilic archaea. They are considered to be primordial enzymes of ATP synthesis in the early evolution of life. We present the first crystal structures, to our knowledge, of an ACD from the hyperthermophilic archaeon Candidatus Korachaeum cryptofilum. These structures reveal a unique arrangement of the ACD subunits alpha and beta within an α2β2-heterotetrameric complex. This arrangement significantly differs from other members of the superfamily. To transmit an activated phosphoryl moiety from the Ac-CoA binding site (within the alpha subunit) to the NDP-binding site (within the beta subunit), a distance of 51 Å has to be bridged. This transmission requires a larger rearrangement within the protein complex involving a 21-aa-long phosphohistidine-containing segment of the alpha subunit. Spatial restraints of the interaction of this segment with the beta subunit explain the necessity for a second highly conserved His residue within the beta subunit. The data support the proposed four-step reaction mechanism of ACDs, coupling acyl-CoA thioesters with ATP synthesis. Furthermore, the determined crystal structure of the complex with bound Ac-CoA allows first insight, to our knowledge, into the determinants for acyl-CoA substrate specificity. The composition and size of loops protruding into the binding pocket of acyl-CoA are determined by the individual arrangement of the characteristic subdomains.
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