Study of the Structure and Biological Activity of the Amino-Terminus of the α-Toxin from Clostridium welchii Type A

Xu, Chi; She, Yuhan; Fu, Fengyang; Lin, Yimin; Chongbo, Xu

doi:10.1007/s00284-019-01733-5

Cited by 1 publication

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“…CpPLC contains three essential Zn +2 atoms in its N-terminal domain, as also observed for B. cereus [21] and L. monocytogenes PLC [13], and these could be removed by ethylenediaminetetraacetic acid (EDTA) or o-phenanthroline. Asp56 is a critical residue in the Zn +2 binding site of CpPLC [22], and the D56G substitution changes the secondary structure and abolishes toxicity [23]. The C-terminal domain (residues 256-370) consists of an eight-stranded antiparallel beta-sandwich required for the Ca +2dependent interaction with substrates [19,24].…”

Section: Structural Features Comparisonmentioning

confidence: 99%

Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase

et al. 2021

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Bacterial phospholipases and sphingomyelinases are lipolytic esterases that are structurally and evolutionarily heterogeneous. These enzymes play crucial roles as virulence factors in several human and animal infectious diseases. Some bacterial phospholipases C (PLCs) have both phosphatidylcholinesterase and sphingomyelinase C activities. Among them, Listeria monocytogenes PlcB, Clostridium perfringens PLC, and Pseudomonas aeruginosa PlcH are the most deeply understood. In silico predictions of substrates docking with these three bacterial enzymes provide evidence that they interact with different substrates at the same active site. This review discusses structural aspects, substrate specificity, and the mechanism of action of those bacterial enzymes on target cells and animal infection models to shed light on their roles in pathogenesis.

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