2lre

The solution structure of the dimeric Acanthaporin

spinqualitylabelsall models 2lre Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lre is a 2 chain structure with sequence from Acanthamoeba culbertsoni. This structure supersedes the now removed PDB entry 2kuj. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I3NI56_9EUKA Publication Abstract from PubMed 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. Structure and function of a unique pore-forming protein from a pathogenic acanthamoeba.,Michalek M, Sonnichsen FD, Wechselberger R, Dingley AJ, Hung CW, Kopp A, Wienk H, Simanski M, Herbst R, Lorenzen I, Marciano-Cabral F, Gelhaus C, Gutsmann T, Tholey A, Grotzinger J, Leippe M Nat Chem Biol. 2013 Jan;9(1):37-42. doi: 10.1038/nchembio.1116. Epub 2012 Nov 11. PMID:23143413 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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