1pre

From Proteopedia

(Difference between revisions)

Revision as of 09:33, 8 September 2021

PROAEROLYSIN

Structural highlights

1pre is a 2 chain structure with sequence from "aeromonas_liquefaciens"_kluyver_and_van_niel_1936 "aeromonas liquefaciens" kluyver and van niel 1936. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AERA_AERHY] Aerolysin is a cytolytic toxin exported by the Gram negative Aeromonas bacteria. The mature toxin binds to eukaryotic cells and aggregates to form holes approximately 3 nm in diameter, leading to destruction of the membrane permeability barrier and osmotic lysis.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Aerolysin is chiefly responsible for the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that destroys sensitive cells by breaking their permeability barriers. Here we describe the structure of proaerolysin determined by X-ray crystallography at 2.8 A resolution. The protoxin (M(r) 52,000) adopts a novel protein fold. Images of an aerolysin oligomer derived from electron microscopy have assisted in constructing a model of the membrane channel and have led to the proposal of a scheme to account for insertion of the protein into lipid bilayers to form ion channels.

Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states.,Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D Nature. 1994 Jan 20;367(6460):292-5. PMID:7510043^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature. 1994 Jan 20;367(6460):292-5. PMID:7510043 doi:http://dx.doi.org/10.1038/367292a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pre"

@@ Line 3: / Line 3: @@
 <StructureSection load='1pre' size='340' side='right'caption='[[1pre]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pre]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"aeromonas_liquefaciens"_kluyver_and_van_niel_1936 "aeromonas liquefaciens" kluyver and van niel 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pre]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"aeromonas_liquefaciens"_kluyver_and_van_niel_1936 "aeromonas liquefaciens" kluyver and van niel 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRE FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pre OCA], [http://pdbe.org/1pre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pre RCSB], [http://www.ebi.ac.uk/pdbsum/1pre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pre ProSAT]</span></td></tr>
+</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=1pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pre OCA], [https://pdbe.org/1pre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pre RCSB], [https://www.ebi.ac.uk/pdbsum/1pre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pre ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AERA_AERHY AERA_AERHY]] Aerolysin is a cytolytic toxin exported by the Gram negative Aeromonas bacteria. The mature toxin binds to eukaryotic cells and aggregates to form holes approximately 3 nm in diameter, leading to destruction of the membrane permeability barrier and osmotic lysis.
+[[https://www.uniprot.org/uniprot/AERA_AERHY AERA_AERHY]] Aerolysin is a cytolytic toxin exported by the Gram negative Aeromonas bacteria. The mature toxin binds to eukaryotic cells and aggregates to form holes approximately 3 nm in diameter, leading to destruction of the membrane permeability barrier and osmotic lysis.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1pre

From Proteopedia

Revision as of 09:33, 8 September 2021

PROAEROLYSIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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