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Figure 7 | BMC Microbiology

Figure 7

From: Diversity and transcription of proteases involved in the maturation of hydrogenases in Nostoc punctiforme ATCC 29133 and Nostocsp. strain PCC 7120

Figure 7

HybD (1CFZ.pdb) from E. coli and the 3D-structure model of HoxW from Nostoc PCC 7120. Illustration showing the crystallised structure of HybD (1CFZ.pdb) from E. coli (top) and the 3D structure model of HoxW from Nostoc PCC 7120 (bottom). A. Ribbon diagram of HybD (E.coli) and HoxW (Nostoc PCC 7120). Colour guide; green: amino acids believed to be involved in binding to the nickel in the active site of the large subunit, orange: the differently conserved residues i.e. the "HOXBOX" in HybD (DGG) and HoxW (HQL). Abbreviations; H: α-helix, S: β-sheet. B. The position of conserved amino acid residues on the surface of a representative of hydrogenase specific proteases from group 1 (HybD-1CFZ.pdb) and 3d (HoxW-3D model). Colour guide; red: residues conserved among all (100%) of the strains within a group, blue: residues found to be conserved or similar among 80% of the strains in each group. C. Protein-protein docking result of hydrogenase specific proteases to the large subunit of the [NiFe]-hydrogenase. HybC (large subunit) and HybD (protease) from E. coli. HoxH (large subunit) and HoxW (protease) from Nostoc PCC 7120. Colour guide; orange: conserved residues, i.e. the "HOXBOX" region, blue: identical and similar residues shared by 80% of the strains in group 1 and group 3d respectively. Light blue arrow indicates direction as seen in (B). Three of the structures (HybC, HoxH and HoxW) were modelled by using the online program SWISS-MODEL. D. Space filling structure of HybC (E. coli). Colour guide; green: active site with the four cysteins involved in the binding of nickel and iron, red: the C-terminal histidine (His552), orange: region on the large subunit which might be in contact with the HOXBOX.

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