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Fig. 6 | BMC Molecular and Cell Biology

Fig. 6

From: Characterization and engineering of a DNA polymerase reveals a single amino-acid substitution in the fingers subdomain to increase strand-displacement activity of A-family prokaryotic DNA polymerases

Fig. 6

Section of sequence alignment between DNA polymerase I large fragment from Geobacillus stearothermophilus (Gbst_polI_LF), Ureibacillus thermosphaericus (Ubts_polI_LF) and Psychrobacillus sp. (PB_polI_LF) with secondary structure elements from Gbst pol I LF on top (PDB code 1XWL). The sequence alignment covers the O-helix, O1-helix and O2-helix including the conserved aspartate residue at position 422 (black triangle) and arginine residue at position 322 (black circle). The multiple sequence alignment has been generated with Clustal Omega [17] and illustrated including secondary structure information with ESPript 3.0 [18]

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BMC Molecular and Cell Biology

ISSN: 2661-8850

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