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5ly6

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Revision as of 03:31, 16 November 2017

CryoEM structure of the membrane pore complex of Pneumolysin at 4.5A

Structural highlights

5ly6 is a 1 chain structure with sequence from Strp2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	ply, SPD_1726 (STRP2)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TACY_STRP2] Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Can be reversibly inactivated by oxidation (By similarity).

Publication Abstract from PubMed

Many pathogenic bacteria produce pore-forming toxins to attack and kill human cells. We have determined the 4.5 A structure of the ~2.2 MDa pore complex of pneumolysin, the main virulence factor of Streptococcus pneumoniae, by cryoEM. The pneumolysin pore is a 400 A ring of 42 membrane-inserted monomers. Domain D3 of the soluble toxin refolds into two ~85 A beta-hairpins that traverse the lipid bilayer and assemble into a 168-strand beta-barrel. The pore complex is stabilized by salt bridges between beta-hairpins of adjacent subunits and an internal alpha-barrel. The apolar outer barrel surface with large sidechains is immersed in the lipid bilayer, while the inner barrel surface is highly charged. Comparison of the cryoEM pore complex to the prepore structure obtained by electron cryo-tomography and the x-ray structure of the soluble form reveals the detailed mechanisms by which the toxin monomers insert into the lipid bilayer to perforate the target membrane.

CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin.,van Pee K, Neuhaus A, D'Imprima E, Mills DJ, Kuhlbrandt W, Yildiz O Elife. 2017 Mar 21;6. pii: e23644. doi: 10.7554/eLife.23644. PMID:28323617^[1]

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

References

↑ van Pee K, Neuhaus A, D'Imprima E, Mills DJ, Kuhlbrandt W, Yildiz O. CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin. Elife. 2017 Mar 21;6. pii: e23644. doi: 10.7554/eLife.23644. PMID:28323617 doi:http://dx.doi.org/10.7554/eLife.23644

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ly6"

@@ Line 3: / Line 3: @@
 <StructureSection load='5ly6' size='340' side='right' caption='[[5ly6]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ly6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LY6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ly6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strp2 Strp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LY6 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=5ly6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ly6 OCA], [http://pdbe.org/5ly6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ly6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ly6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ly6 ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ply, SPD_1726 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=373153 STRP2])</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=5ly6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ly6 OCA], [http://pdbe.org/5ly6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ly6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ly6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ly6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Strp2]]
 [[Category: Imprima, E D]]
 [[Category: Kuehlbrandt, W]]

5ly6

From Proteopedia

Revision as of 03:31, 16 November 2017

CryoEM structure of the membrane pore complex of Pneumolysin at 4.5A

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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