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Fig. 2 | Annals of Clinical Microbiology and Antimicrobials

Fig. 2

From: Purification and characterization of a new β-lactamase OXA-205 from Pseudomonas aeruginosa

Fig. 2

Amino acid sequence comparison of OXA-205 with the representatives of the OXA-2 lineage. Sequences of OXA-46 [GenBank:AAN63499.1] OXA-2 [GenBank:CAC82805.1]; OXA-3 [GenBank:AAC41449.1]; OXA-20 [GenBank:CAA30246.1]; OXA-53 [GenBank:AAP43641.1]; Bce (OXA-119), an OXA-type enzyme from Burkholderia cepacia clinical isolate from Ireland [GenBank:AAK55330.1]; OXA-PMW (OXA-118), an OXA-type enzyme encoded by a plasmid from an unidentified bacterium from a wastewater treatment plant in Germany [GenBank:AAN41427.1) are shown. The structural elements of chain C of OXA-46 enzyme (PDB:3IF6) are shown above the sequence: α, α-helices; β, β-strands; η, 3/10-helix. Predicted 21-amino acid N-terminal signal peptide is marked by black rectangles below the alignment. Identical residues are shaded in black. Black bald characters mark similar residues. Typical conserved motifs of class D enzymes are marked by the asterisk below the alignment [4]. Residues that are predicted to be involved in the dimerisation are shown by triangles. Residues are numbered according to class D β-lactamase (DBL) numbering [25]

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