3o39

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<StructureSection load='3o39' size='340' side='right'caption='[[3o39]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3o39' size='340' side='right'caption='[[3o39]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3o39]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_0157:h7_edl933 Escherichia coli 0157:h7 edl933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O39 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3o39]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._EDL933 Escherichia coli O157:H7 str. EDL933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O39 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.599&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECs2449, spy, Z2775 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155864 Escherichia coli 0157:H7 EDL933])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o39 OCA], [https://pdbe.org/3o39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o39 RCSB], [https://www.ebi.ac.uk/pdbsum/3o39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o39 ProSAT]</span></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=3o39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o39 OCA], [https://pdbe.org/3o39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o39 RCSB], [https://www.ebi.ac.uk/pdbsum/3o39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o39 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SPY_ECO57 SPY_ECO57] An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region. Protect proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898).<ref>PMID:21317898</ref>
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To optimize the in vivo folding of proteins, we linked protein stability to antibiotic resistance, thereby forcing bacteria to effectively fold and stabilize proteins. When we challenged Escherichia coli to stabilize a very unstable periplasmic protein, it massively overproduced a periplasmic protein called Spy, which increases the steady-state levels of a set of unstable protein mutants up to 700-fold. In vitro studies demonstrate that the Spy protein is an effective ATP-independent chaperone that suppresses protein aggregation and aids protein refolding. Our strategy opens up new routes for chaperone discovery and the custom tailoring of the in vivo folding environment. Spy forms thin, apparently flexible cradle-shaped dimers. The structure of Spy is unlike that of any previously solved chaperone, making it the prototypical member of a new class of small chaperones that facilitate protein refolding in the absence of energy cofactors.
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Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.,Quan S, Koldewey P, Tapley T, Kirsch N, Ruane KM, Pfizenmaier J, Shi R, Hofmann S, Foit L, Ren G, Jakob U, Xu Z, Cygler M, Bardwell JC Nat Struct Mol Biol. 2011 Feb 13. PMID:21317898<ref>PMID:21317898</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3o39" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli 0157:h7 edl933]]
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[[Category: Escherichia coli O157:H7 str. EDL933]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Cygler M]]
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[[Category: Cygler, M]]
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[[Category: Ruane KM]]
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[[Category: Ruane, K M]]
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[[Category: Shi R]]
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[[Category: Shi, R]]
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[[Category: Alpha-helical]]
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[[Category: Bsgi]]
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[[Category: Chaperone]]
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Revision as of 10:03, 14 February 2024

Crystal Structure of SPY

PDB ID 3o39

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