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Figure 1 | BMC Bioinformatics

Figure 1

From: Structure and computational analysis of a novel protein with metallopeptidase-like and circularly permuted winged-helix-turn-helix domains reveals a possible role in modified polysaccharide biosynthesis

Figure 1

Crystal structure and domain architecture. The crystal structure of CA_C2195 from Clostridium acetobutyliticum, with the N- and C-termini labeled as ‘;N’ and ‘;C’, reveals 3 domains: residues 1–55 (blue) and 165–355 (yellow) form the N-terminal metallopeptidase domain, DUF4910; residues 56–164 (grey) form the DUF2172 domain; and residues 356–434 (red) form a C-terminal wHTH domain, HTH_47. Residues in the putative active site are Asp195 (red stick); and His189 and His324 (cyan sticks), and they are bound to a Zn ion from the crystallization condition. Imidazole from the crystallization condition is also bound to the active site Zn. The lower panel is a linear representation of the domain architecture of CA_C2195.

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BMC Bioinformatics

ISSN: 1471-2105

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