Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sites

Download
  1. Get@NRC: Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sites (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1016/j.str.2011.09.023
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeArticle
Journal titleStructure
ISSN0969-2126
Volume19
Issue12
Pages17731783; # of pages: 11
Subjectbacterial protein; hydrogenase; HypF protein; Kae1 protein; unclassified drug; YrdC protein; zinc finger protein; zinc ion; amino terminal sequence; article; carbamoylation; carboxy terminal sequence; enzyme activity; Escherichia coli; mutation; nonhuman; nucleotide binding site; priority journal; 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
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.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Biotechnology Research Institute (BRI-IRB)
Peer reviewedYes
NPARC number21271571
Export citationExport as RIS
Report a correctionReport a correction
Record identifiercc894fb4-da4a-43da-88bd-761acd2a7dba
Record created2014-03-24
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)