1k3s: Difference between revisions
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New page: left|200px<br /><applet load="1k3s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k3s, resolution 1.9Å" /> '''Type III Secretion Ch... |
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== | ==Type III Secretion Chaperone SigE== | ||
Several Gram-negative bacterial pathogens have evolved a type III | <StructureSection load='1k3s' size='340' side='right'caption='[[1k3s]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1k3s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K3S FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1k3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k3s OCA], [https://pdbe.org/1k3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k3s RCSB], [https://www.ebi.ac.uk/pdbsum/1k3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k3s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0F6AZQ4_SALT1 A0A0F6AZQ4_SALT1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Several Gram-negative bacterial pathogens have evolved a type III secretion system to deliver virulence effector proteins directly into eukaryotic cells, a process essential for disease. This specialized secretion process requires customized chaperones specific for particular effector proteins. The crystal structures of the enterohemorrhagic Escherichia coli O157:H7 Tir-specific chaperone CesT and the Salmonella enterica SigD-specific chaperone SigE reveal a common overall fold and formation of homodimers. Site-directed mutagenesis suggests that variable, delocalized hydrophobic surfaces observed on the chaperone homodimers are responsible for specific binding to a particular effector protein. Isothermal titration calorimetry studies of Tir-CesT and enzymatic activity profiles of SigD-SigE indicate that the effector proteins are not globally unfolded in the presence of their cognate chaperones. | |||
Structural and biochemical characterization of the type III secretion chaperones CesT and SigE.,Luo Y, Bertero MG, Frey EA, Pfuetzner RA, Wenk MR, Creagh L, Marcus SL, Lim D, Sicheri F, Kay C, Haynes C, Finlay BB, Strynadka NC Nat Struct Biol. 2001 Dec;8(12):1031-6. PMID:11685226<ref>PMID:11685226</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1k3s" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Salmonella enterica]] | [[Category: Salmonella enterica]] | ||
[[Category: Bertero MG]] | |||
[[Category: Bertero | [[Category: Creagh L]] | ||
[[Category: Creagh | [[Category: Finlay BB]] | ||
[[Category: Finlay | [[Category: Frey EA]] | ||
[[Category: Frey | [[Category: Lim D]] | ||
[[Category: Lim | [[Category: Luo Y]] | ||
[[Category: Luo | [[Category: Marcus SL]] | ||
[[Category: Marcus | [[Category: Pfuetzner RA]] | ||
[[Category: Pfuetzner | [[Category: Strynadka NCJ]] | ||
[[Category: Strynadka | [[Category: Wenk MR]] | ||
[[Category: Wenk | |||
Latest revision as of 13:00, 21 June 2023
Type III Secretion Chaperone SigEType III Secretion Chaperone SigE
Structural highlights
FunctionPublication Abstract from PubMedSeveral Gram-negative bacterial pathogens have evolved a type III secretion system to deliver virulence effector proteins directly into eukaryotic cells, a process essential for disease. This specialized secretion process requires customized chaperones specific for particular effector proteins. The crystal structures of the enterohemorrhagic Escherichia coli O157:H7 Tir-specific chaperone CesT and the Salmonella enterica SigD-specific chaperone SigE reveal a common overall fold and formation of homodimers. Site-directed mutagenesis suggests that variable, delocalized hydrophobic surfaces observed on the chaperone homodimers are responsible for specific binding to a particular effector protein. Isothermal titration calorimetry studies of Tir-CesT and enzymatic activity profiles of SigD-SigE indicate that the effector proteins are not globally unfolded in the presence of their cognate chaperones. Structural and biochemical characterization of the type III secretion chaperones CesT and SigE.,Luo Y, Bertero MG, Frey EA, Pfuetzner RA, Wenk MR, Creagh L, Marcus SL, Lim D, Sicheri F, Kay C, Haynes C, Finlay BB, Strynadka NC Nat Struct Biol. 2001 Dec;8(12):1031-6. PMID:11685226[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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