View source for 2lrd


==The solution structure of the monomeric Acanthaporin==
<StructureSection load='2lrd' size='340' side='right'caption='[[2lrd]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lrd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_culbertsoni Acanthamoeba culbertsoni]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ku8 2ku8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LRD FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lrd OCA], [https://pdbe.org/2lrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lrd RCSB], [https://www.ebi.ac.uk/pdbsum/2lrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lrd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I3NI56_9EUKA I3NI56_9EUKA] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:23143413</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lrd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acanthamoeba culbertsoni]]
[[Category: Large Structures]]
[[Category: Dingley AJ]]
[[Category: Gelhaus C]]
[[Category: Groetzinger J]]
[[Category: Herbst R]]
[[Category: Leippe M]]
[[Category: Lorenzen I]]
[[Category: Marciano-Cabral F]]
[[Category: Michalek M]]
[[Category: Simanski M]]
[[Category: Soennichsen FD]]
[[Category: Wechselberger R]]
[[Category: Wienk H]]