ArticleThe Journal of biological chemistry2012
Structural basis for the reaction mechanism of S-carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 49 citations in OpenAlex.
- Biosynthesis and assembly of hydrogenase [NiFe]-cofactor: recent advances and perspectives.Metallomics : integrated biometal science · 2025Review
- Structure-function analysis of an ancient TsaD-TsaC-SUA5-TcdA modular enzyme reveals a prototype of tRNA t6A and ct6A synthetases.Nucleic acids research · 2023Article
- Conservation and Diversification of tRNA tInternational journal of molecular sciences · 2022Review
- Endowing homodimeric carbamoyltransferase GdmN with iterative functions through structural characterization and mechanistic studies.Nature communications · 2022Article
- Efficient anaerobic consumption of D-xylose by E. coli BL21(DE3) via xylR adaptive mutation.BMC microbiology · 2021Article
- Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly.The Biochemical journal · 2021Article
- Targeting adenylate-forming enzymes with designed sulfonyladenosine inhibitors.The Journal of antibiotics · 2019Review
- Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.Communications biology · 2019Article
- Sources and Fates of Carbamyl Phosphate: A Labile Energy-Rich Molecule with Multiple Facets.Biology · 2018Review
- Proteolytic cleavage orchestrates cofactor insertion and protein assembly in [NiFe]-hydrogenase biosynthesis.The Journal of biological chemistry · 2017Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
- Distribution of Hydrogenases in Cyanobacteria: A Phylum-Wide Genomic Survey.Frontiers in genetics · 2016Article
- Coordination of Synthesis and Assembly of a Modular Membrane-Associated [NiFe]-Hydrogenase Is Determined by Cleavage of the C-Terminal Peptide.Journal of bacteriology · 2015Article
- Article
- The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.PloS one · 2014Article
- Crystal structures of the carbamoylated and cyanated forms of HypE for [NiFe] hydrogenase maturation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification.Nucleic acids research · 2013Article
- Dual role of HupF in the biosynthesis of [NiFe] hydrogenase in Rhizobium leguminosarum.BMC microbiology · 2012Article
- Structure of the [NiFe]-hydrogenase maturation protein HypF from Thermococcus kodakarensis KOD1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
As a remarkable structural feature of hydrogenase active sites, [NiFe]-hydrogenases harbor one carbonyl and two cyano ligands, where HypE and HypF are involved in the biosynthesis of the nitrile group as a precursor of the cyano groups. HypF catalyzes S-carbamoylation of the C-terminal cysteine of HypE via three steps using carbamoylphosphate and ATP, producing two unstable intermediates: carbamate and carbamoyladenylate. Although the crystal structures of intact HypE homodimers and partial HypF have been reported, it remains unclear how the consecutive reactions occur without the loss of unstable intermediates during the proposed reaction scheme. Here we report the crystal structures of full-length HypF both alone and in complex with HypE at resolutions of 2.0 and 2.6 Å, respectively. Three catalytic sites of the structures of the HypF nucleotide- and phosphate-bound forms have been identified, with each site connected via channels inside the protein. This finding suggests that the first two consecutive reactions occur without the release of carbamate or carbamoyladenylate from the enzyme. The structure of HypF in complex with HypE revealed that HypF can associate with HypE without disturbing its homodimeric interaction and that the binding manner allows the C-terminal Cys-351 of HypE to access the S-carbamoylation active site in HypF, suggesting that the third step can also proceed without the release of carbamoyladenylate. A comparison of the structure of HypF with the recently reported structures of O-carbamoyltransferase revealed different reaction mechanisms for carbamoyladenylate synthesis and a similar reaction mechanism for carbamoyltransfer to produce the carbamoyl-HypE molecule.
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