1cfz | pdb_00001cfz

HYDROGENASE MATURATING ENDOPEPTIDASE HYBD FROM E. COLI

spinqualitylabelsall models 1cfz, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cfz is a 6 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [HYBD_ECOLI] Protease involved in the C-terminal processing of HybC, the large subunit of hydrogenase 2. Specifically cleaves off a 15 amino acid peptide from the C-terminus of the precursor of HybC. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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