Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT
Figure 6
(a) Amino acid sequence alignment of KpDnaT. An alignment consensus of 29 sequenced DnaT homologs by the program ConSurf reveals the degree of variability at each position along the primary sequence. In general, the amino acid residues in the C-terminal region of KpDnaT are highly conserved. (b) Modeled structure of KpDnaT. The structure of KpDnaT is modeled by the bioinformatic program (PS)2 and then manually built using threefold symmetry with a 25 mer ssDNA (gold). The highly conserved hydrophobic (green) and basic residues (blue) of KpDnaT, His136, His137, Trp140, Lys143, Arg146, and Arg151 located on the potential ssDNA-binding surface are indicated.
