| DOI | Resolve DOI: https://doi.org/10.1016/j.str.2011.09.023 |
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| Author | Search for: Petkun, S.; Search for: Shi, R.; Search for: Li, Y.1; Search for: Asinas, A.; Search for: Munger, C.; Search for: Zhang, L.; Search for: Waclawek, M.; Search for: Soboh, B.; Search for: Sawers, R.G.; Search for: Cygler, M.1 |
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| Affiliation | - National Research Council of Canada. NRC Biotechnology Research Institute
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| Format | Text, Article |
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| Subject | 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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| Abstract | [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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| Publication date | 2011 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 21271571 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | cc894fb4-da4a-43da-88bd-761acd2a7dba |
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| Record created | 2014-03-24 |
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| Record modified | 2022-11-18 |
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