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Figure 7 | BMC Bioinformatics

Figure 7

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 7

Comparison of wHTH domains. (A) The circularly permuted wHTH domain observed in CA_C2195 (red, left panel) resembles another circularly permuted wHTH domain present in the structure of a Peptidase_M24 family aminopeptidase [PDB:1boa] (red, right panel), and may be involved in substrate recognition and specificity. (B) The wHTH domain in CA_C2195 (left) is compared to the wHTH domain from Peptidase_M24 [PDB:1boa] (center) and a wHTH domain from a transcription factor [PDB:1cf7] (right), which was one of the proteins most similar in structure to the CA_C2195 wHTH domain. Each domain is colored from the N-terminus (blue) to the C-terminus (red). All domains are in a similar orientation. (C) Topology diagrams for the three domains in (B) in the same order depicting the arrangement of secondary structure elements and circular permutation in the CA_C2195 wHTH compared to the transcription factor wHTH. Cylinders represent α-helices, arrows represent β-strands and the N- and C-termini are labeled.

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BMC Bioinformatics

ISSN: 1471-2105

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