Summary for 2LRD
| Entry DOI | 10.2210/pdb2lrd/pdb |
| Related | 2LRE |
| NMR Information | BMRB: 18357 |
| Descriptor | Acanthaporin (1 entity in total) |
| Functional Keywords | pore-forming toxin, alpha helix, antimicrobial protein |
| Biological source | Acanthamoeba culbertsoni |
| Total number of polymer chains | 1 |
| Total formula weight | 6001.23 |
| Authors | Michalek, M.,Soennichsen, F.D.,Wechselberger, R.,Dingley, A.J.,Wienk, H.,Simanski, M.,Herbst, R.,Lorenzen, I.,Marciano-Cabral, F.,Gelhaus, C.,Groetzinger, J.,Leippe, M. (deposition date: 2012-03-28, release date: 2012-05-02, Last modification date: 2023-06-14) |
| Primary citation | Michalek, M.,Sonnichsen, F.D.,Wechselberger, R.,Dingley, A.J.,Hung, C.W.,Kopp, A.,Wienk, H.,Simanski, M.,Herbst, R.,Lorenzen, I.,Marciano-Cabral, F.,Gelhaus, C.,Gutsmann, T.,Tholey, A.,Grotzinger, J.,Leippe, M. Structure and function of a unique pore-forming protein from a pathogenic acanthamoeba. Nat.Chem.Biol., 9:37-42, 2013 Cited by PubMed Abstract: Human pathogens often produce soluble protein toxins that generate pores inside membranes, resulting in the death of target cells and tissue damage. In pathogenic amoebae, this has been exemplified with amoebapores of the enteric protozoan parasite Entamoeba histolytica. Here we characterize acanthaporin, to our knowledge the first pore-forming toxin to be described from acanthamoebae, which are free-living, bacteria-feeding, unicellular organisms that are opportunistic pathogens of increasing importance and cause severe and often fatal diseases. We isolated acanthaporin from extracts of virulent Acanthamoeba culbertsoni by tracking its pore-forming activity, molecularly cloned the gene of its precursor and recombinantly expressed the mature protein in bacteria. Acanthaporin was cytotoxic for human neuronal cells and exerted antimicrobial activity against a variety of bacterial strains by permeabilizing their membranes. The tertiary structures of acanthaporin's active monomeric form and inactive dimeric form, both solved by NMR spectroscopy, revealed a currently unknown protein fold and a pH-dependent trigger mechanism of activation. PubMed: 23143413DOI: 10.1038/nchembio.1116 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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