| DOI | Trouver le DOI : https://doi.org/10.1016/j.str.2011.09.023 |
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| Auteur | Rechercher : Petkun, S.; Rechercher : Shi, R.; Rechercher : Li, Y.1; Rechercher : Asinas, A.; Rechercher : Munger, C.; Rechercher : Zhang, L.; Rechercher : Waclawek, M.; Rechercher : Soboh, B.; Rechercher : Sawers, R.G.; Rechercher : Cygler, M.1 |
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| Affiliation | - Conseil national de recherches du Canada. Institut de recherche en biotechnologie du CNRC
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| Format | Texte, Article |
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| Sujet | bacterial protein; hydrogenase; HypF protein; Kae1 protein; unclassified drug; YrdC protein; zinc finger protein; zinc ion; amino terminal sequence; carbamoylation; carboxy terminal sequence; enzyme activity; Escherichia coli; mutation; nucleotide binding site; protein binding; protein domain; protein processing; protein structure; Acid Anhydride Hydrolases; Binding Sites; Carbamyl Phosphate; Carboxyl and Carbamoyl Transferases; Catalysis; Catalytic Domain; Escherichia coli; Escherichia coli Proteins; Hydrogenase; Ligands |
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| Résumé | [NiFe]-hydrogenases are multimeric proteins. The large subunit contains the NiFe(CN) 2CO bimetallic active center and the small subunit contains Fe-S clusters. Biosynthesis and assembly of the NiFe(CN) 2CO active center requires six Hyp accessory proteins. The synthesis of the CN - ligands is catalyzed by the combined actions of HypF and HypE using carbamoylphosphate as a substrate. We report the structure of Escherichia coli HypF(92-750) lacking the N-terminal acylphosphatase domain. HypF(92-750) comprises the novel Zn-finger domain, the nucleotide-binding YrdC-like domain, and the Kae1-like universal domain, also binding a nucleotide and a Zn 2+ ion. The two nucleotide-binding sites are sequestered in an internal cavity, facing each other and separated by ∼14 . The YrdC-like domain converts carbamoyl moiety to a carbamoyl adenylate intermediate, which is channeled to the Kae1-like domain. Mutations within either nucleotide-binding site compromise hydrogenase maturation but do not affect the carbamoylphosphate phosphatase activity. © 2011 Elsevier Ltd All rights reserved. |
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| Date de publication | 2011 |
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| Dans | |
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| Langue | anglais |
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| Publications évaluées par des pairs | Oui |
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| Numéro NPARC | 21271571 |
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| Exporter la notice | Exporter en format RIS |
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| Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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| Identificateur de l’enregistrement | cc894fb4-da4a-43da-88bd-761acd2a7dba |
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| Enregistrement créé | 2014-03-24 |
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| Enregistrement modifié | 2022-11-18 |
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