Skip to main content
Figure 1 | BMC Structural Biology

Figure 1

From: Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface

Figure 1

Sequence analysis of acetokinase family of enzymes. Multiple sequence alignment of St AckA with known structures belonging to acetokinase family. Sequence code: St AckA, S. typhimurium AckA; Tm AckA, Thermotoga maritima AckA; Mt AckA, Methanosarcina thermophila AckA; Ma AckA, Mycobacterium avium AckA; Ft TdcD, Francisella tularensis putative acetate/propionate kinase; St TdcD, S. typhimurium propionate kinase; Tm Buk2, Thermotoga maritima butyrate kinase 2. All sequences are numbered at the beginning of each block of aligned sequences. St AckA numbering is indicated by every 10 residues using a dot symbol on top of the alignment. Secondary structures of Form-I St AckA and Tm Buk2 (PDB:1SAZ) aligned onto their respective sequences are also shown (refer Figure 3A for secondary structure labeling scheme). Colour code: strictly conserved residues are shown in yellow with black background; highly similar regions are shown in blue with grey background. Putative acetate and nucleotide binding residues are marked with orange rhombi and magenta circles, respectively. Residues interacting with citrate in Form-II St AckA structure are highlighted by green triangles.

Back to article page