1cfz
HYDROGENASE MATURATING ENDOPEPTIDASE HYBD FROM E. COLI
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OverviewOverview
The maturation of [NiFe] hydrogenases includes formation of the nickel, metallocenter, proteolytic processing of the metal center carrying large, subunit, and its assembling with other hydrogenase subunits. The, hydrogenase maturating enzyme HYBD from Escherichia coli, a protease of, molecular mass 17.5 kDa, specifically cleaves off a 15 amino acid peptide, from the C terminus of the precursor of the large subunit of hydrogenase 2, in a nickel-dependent manner. Here we report the crystal structure of HYBD, at 2.2 A resolution. It consists of a twisted five-stranded beta-sheet, surrounded by four and three helices, respectively, on each side. A, cadmium ion from the crystallization buffer binds to the proposed, nickel-binding site and is penta-coordinated by Glu16, Asp62, His93, and a, water molecule in a pseudo-tetragonal arrangement. HYBD is topologically, related to members of the metzincins superfamily of zinc endoproteinases, sharing the central beta-sheet and three helices. In contrast to the, metzincins, the metal-binding site of HYBD is localized at the C-terminal, end of the beta-sheet. Three helical insertions unique to HYBD pack, against one side of the sheet, build up the active site cleft, and provide, His93 as ligand to the metal. From this structure, we derive molecular, clues into how the protease HYBD is involved in the hydrogenase maturation, process.
About this StructureAbout this Structure
1CFZ is a Single protein structure of sequence from Escherichia coli with CD as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli., Fritsche E, Paschos A, Beisel HG, Bock A, Huber R, J Mol Biol. 1999 May 21;288(5):989-98. PMID:10331925
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