Figure 2: Sequence alignment of select bacterial L-asparaginases. | Scientific Reports

Figure 2: Sequence alignment of select bacterial L-asparaginases.

From: The differential ability of asparagine and glutamine in promoting the closed/active enzyme conformation rationalizes the Wolinella succinogenes L-asparaginase substrate specificity

Figure 2

Despite the key function of the flexible N-terminal loop (boundaries indicated by square bracket), amino acid sequence conservation is limited to the first segment, to the tyrosine that approaches the ligand (Tyr27 in WoA), and several hydrophobic residues. In this alignment, the strictly and mostly conserved residues are highlighted in red and yellow, respectively. Open circles indicate conserved hydrophobic residues stabilizing the N-terminal loop in one or both conformations. Blue stars and orange arrows indicate conserved hydrophobic residues stabilizing the loop in its closed/active and open/inactive conformations, respectively. Red boxes indicate conserved hydrophobic backbone residues stabilizing the internal-hinge, Ile15 in WoA. Blue arrow shows the amino acid at position 121st in WoA. The secondary structure shown above the primary sequence is based on the WoA-P121 + Asp structure (PDB ID 5K3O). Numbering is based on WoA sequence. The UniProt entries of corresponding crystal structures used for this alignment are: Wolinella succinogenes L-asparaginase, WoA-S121 + Asp_5K4G, P50286; Escherichia coli L-asparaginase, EcA_3ECA, P00805; Erwinia chrysanthemi L-asparaginase, ErA_5F52, P06608; Erwinia carotovora L-asparaginase, EtA_2HLN, Q6Q4F4; Helicobacter pylori L-asparaginase, HpA_2WLT, O25424; Pseudomonas sp. L-asparaginase, PgA_3PGA, P10182 and Acinetobacter glutaminasificans L-asparaginase, AgA_1AGX, P10172.

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