Helicases sequence conservation

Figure 27.18. Conserved Residues among Helicases. A comparison of the amino acid sequences of hundreds of helicases revealed seven regions of strong sequence conservation (shown in color). When mapped onto the structure of PcrA, these conserved regions lie along the interface between the A1 and B1 domains and along the ATP binding surface.

Fig. 4. Primary structure of reverse gyrases. (A) Schematic representation of reverse gyrase sequence with its two domains comparison of the N-terminal domain with various helicases. elF4A is an eukaryotic initiation factor for translation [J. P. Nielson and H. Trachsel, EMBOJ. 7,2097 (1988)]. PriA is a component of the primosome in bacteria (P Nurse, R. J. DiGate, K. H. Zavitz, and K. J. Marians, Proc. Natl. Acad. Sci. U.S.A. 87,4615 (1990)). Sgsl is a helicase interacting with topoisomerases II and III in yeast [S. Gangloff, J. P McDonald, C. Bendixen, L. Arthur, and R. Rothstein, Mol. Cell Biol. 14, 8391 (1994)]. (B). Amino acid sequences of the helicase motifs in reverse gyrases. x indicates a hydrophobic residue. The sequences shown are a consensus where at least four positions out of six are conserved in reverse gyrases.

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