Figure 1: Multiple sequence alignment of peptidoglycan deacetylase domains of selected peptidoglycan N-deacetylases with secondary structure elements of Bd3279. | Scientific Reports

Figure 1: Multiple sequence alignment of peptidoglycan deacetylase domains of selected peptidoglycan N-deacetylases with secondary structure elements of Bd3279.

From: Interrupting peptidoglycan deacetylation during Bdellovibrio predator-prey interaction prevents ultimate destruction of prey wall, liberating bacterial-ghosts

Figure 1

PgdA = S. pneumoniae R6 PgdA; PdaA = B. subtilis 168 PdaA; Bd0468/Bd3279 = B. bacteriovorus HD100 Bd0468 and Bd3279; BDW12005 = B. bacteriovorus strain W Bd3279 homologue; JSS1865 = Bdellovibrio exovorus JSS Bd3279 homologue. Conserved metal binding residues are indicated by filled ellipses, conserved substrate binding residues are indicated by open ellipses, putative α-hydroxy-proline denoted with star, lipobox colored with green band, disordered active site loop colored with orange band. Sequences were aligned using ClustalW, and the output generated using ESPript47.

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