Journal
STRUCTURE
Volume 19, Issue 12, Pages 1773-1783Publisher
CELL PRESS
DOI: 10.1016/j.str.2011.09.023
Keywords
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Funding
- NSERC
- NRC
- Canadian Institutes of Health Research (CIHR) [GSP-48370]
- University of Saskatchewan
- Deutsche Forschungsgemeinschaft [SA 494/3-1]
- MLU Halle
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[NiFe]-hydrogenases are multimeric proteins. The large subunit contains the NiFe(CN)(2)CO bimetallic active center and the small subunit contains Fe-S clusters. Biosynthesis and assembly of the NiFe(CN)(2)CO 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 Zn2+ ion. The two nucleotide-binding sites are sequestered in an internal cavity, facing each other and separated by similar to 14 angstrom. 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.
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