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Figure 4 | BMC Bioinformatics

Figure 4

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 4

Comparison of the DUF2172 and PA domains. (A) The DUF2172 domain in CA_C2195 (grey, left panel) bears some fold resemblance to the PA (Protease-associated) domain (grey, right panel), which has been observed in a Peptidase_M28 family member [PDB:2ek8, right panel) even though there is no discernible sequence identity. Analogous to the proposed role of the PA domain, the DUF2172 domain may be forming a lid modulating access to the peptidase active site and may also be involved in substrate recognition and specificity. Molecules in the panels are oriented such that the peptidase domains in both superimpose. The active sites in both molecules are shown in cyan sticks and black spheres. (B) A large substructure of the PA domain fold (yellow, left panel) is replaced with a turn of α-helix in DUF2172 (orange, right panel).

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BMC Bioinformatics

ISSN: 1471-2105

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