4p24: Difference between revisions

(6 intermediate revisions by the same user not shown)

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 4p24 is ~~ON HOLD~~

==pore forming toxin==

== Structural highlights ==

<table><tr><td colspan='2'>[[4p24]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P24 FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=4p24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p24 OCA], [https://pdbe.org/4p24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p24 RCSB], [https://www.ebi.ac.uk/pdbsum/4p24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p24 ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/A0A0J9X1Z2_STAAM A0A0J9X1Z2_STAAM]

== Publication Abstract from PubMed ==

Staphylococcal alpha-hemolysin (alpha-HL) is a beta-barrel pore-forming toxin (PFT) expressed by Staphylococcus aureus. alpha-HL is secreted as a water-soluble monomeric protein, which binds to target membranes and forms membrane-inserted heptameric pores. To explore the pore-forming mechanism of alpha-HL in detail, we determined the crystal structure of the alpha-HL monomer and prepore using H35A mutant and W179A/R200A mutant, respectively. Although the overall structure of the monomer was similar to that of other staphylococcal PFTs, a marked difference was observed in the N-terminal amino latch, which bent toward the prestem. Moreover, the prestem was fastened by the cap domain with a key hydrogen bond between Asp45 and Tyr118. Prepore structure showed that the transmembrane region is roughly formed with flexibility, although the upper half of the beta-barrel is formed appropriately. Structure comparison among monomer, prepore and pore revealed a series of motions, in which the N-terminal amino latch released upon oligomerization destroys its own key hydrogen bond betweem Asp45-Try118. This action initiated the protrusion of the prestem. Y118F mutant and the N-terminal truncated mutant markedly decreased in the hemolytic activity, indicating the importance of the key hydrogen bond and the N-terminal amino latch on the pore formation. Based on these observations, we proposed a dynamic molecular mechanism of pore formation for alpha-HL.

~~Authors:~~ Sugawara, T., Yamashita, D., ~~Tanaka~~, Y., Tanaka, I., ~~Yao, M~~.

Structural basis for pore-forming mechanism of staphylococcal alpha-hemolysin.,Sugawara T, Yamashita D, Kato K, Peng Z, Ueda J, Kaneko J, Kamio Y, Tanaka Y, Yao M Toxicon. 2015 Sep 28. pii: S0041-0101(15)30093-3. doi:, 10.1016/j.toxicon.2015.09.033. PMID:26428390<ref>PMID:26428390</ref>

~~Description~~: ~~pore forming toxin~~

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

</div>

==See Also==

*[[Hemolysin 3D structures|Hemolysin 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Staphylococcus aureus subsp. aureus Mu50]]

[[Category: Sugawara T]]

[[Category: Tanaka I]]

[[Category: Tanaka Y]]

[[Category: Yamashita D]]

[[Category: Yao M]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4p24 is ON HOLD
+==pore forming toxin==
+<StructureSection load='4p24' size='340' side='right'caption='[[4p24]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4p24]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P24 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=4p24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p24 OCA], [https://pdbe.org/4p24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p24 RCSB], [https://www.ebi.ac.uk/pdbsum/4p24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p24 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A0J9X1Z2_STAAM A0A0J9X1Z2_STAAM]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Staphylococcal alpha-hemolysin (alpha-HL) is a beta-barrel pore-forming toxin (PFT) expressed by Staphylococcus aureus. alpha-HL is secreted as a water-soluble monomeric protein, which binds to target membranes and forms membrane-inserted heptameric pores. To explore the pore-forming mechanism of alpha-HL in detail, we determined the crystal structure of the alpha-HL monomer and prepore using H35A mutant and W179A/R200A mutant, respectively. Although the overall structure of the monomer was similar to that of other staphylococcal PFTs, a marked difference was observed in the N-terminal amino latch, which bent toward the prestem. Moreover, the prestem was fastened by the cap domain with a key hydrogen bond between Asp45 and Tyr118. Prepore structure showed that the transmembrane region is roughly formed with flexibility, although the upper half of the beta-barrel is formed appropriately. Structure comparison among monomer, prepore and pore revealed a series of motions, in which the N-terminal amino latch released upon oligomerization destroys its own key hydrogen bond betweem Asp45-Try118. This action initiated the protrusion of the prestem. Y118F mutant and the N-terminal truncated mutant markedly decreased in the hemolytic activity, indicating the importance of the key hydrogen bond and the N-terminal amino latch on the pore formation. Based on these observations, we proposed a dynamic molecular mechanism of pore formation for alpha-HL.
-Authors: Sugawara, T., Yamashita, D., Tanaka, Y., Tanaka, I., Yao, M.
+Structural basis for pore-forming mechanism of staphylococcal alpha-hemolysin.,Sugawara T, Yamashita D, Kato K, Peng Z, Ueda J, Kaneko J, Kamio Y, Tanaka Y, Yao M Toxicon. 2015 Sep 28. pii: S0041-0101(15)30093-3. doi:, 10.1016/j.toxicon.2015.09.033. PMID:26428390<ref>PMID:26428390</ref>
-Description: pore forming toxin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4p24" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Hemolysin 3D structures|Hemolysin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Staphylococcus aureus subsp. aureus Mu50]]
+[[Category: Sugawara T]]
+[[Category: Tanaka I]]
+[[Category: Tanaka Y]]
+[[Category: Yamashita D]]
+[[Category: Yao M]]