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| | ==Structural analysis of a chaperone in type III secretion system== | | ==Structural analysis of a chaperone in type III secretion system== |
| - | <StructureSection load='2lhk' size='340' side='right' caption='[[2lhk]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='2lhk' size='340' side='right'caption='[[2lhk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lhk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LHK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lhk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LHK 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=2lhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhk OCA], [http://pdbe.org/2lhk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lhk RCSB], [http://www.ebi.ac.uk/pdbsum/2lhk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lhk ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhk OCA], [https://pdbe.org/2lhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lhk RCSB], [https://www.ebi.ac.uk/pdbsum/2lhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lhk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O52124_ECOLX O52124_ECOLX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Chen, L]] | + | [[Category: Large Structures]] |
| - | [[Category: Economou, A]] | + | [[Category: Chen L]] |
| - | [[Category: Kalodimos, C G]] | + | [[Category: Economou A]] |
| - | [[Category: Chaperone]] | + | [[Category: Kalodimos CG]] |
| - | [[Category: Helical bundle]]
| + | |
| - | [[Category: Type iii secretion system]]
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| Structural highlights
Function
O52124_ECOLX
Publication Abstract from PubMed
Protein-protein interactions mediate a vast number of cellular processes. Here, we present a regulatory mechanism in protein-protein interactions mediated by finely tuned structural instability and coupled with molecular mimicry. We show that a set of type III secretion (TTS) autoinhibited homodimeric chaperones adopt a molten globule-like state that transiently exposes the substrate binding site as a means to become rapidly poised for binding to their cognate protein substrates. Packing defects at the homodimeric interface stimulate binding, whereas correction of these defects results in less labile chaperones that give rise to nonfunctional biological systems. The protein substrates use structural mimicry to offset the weak spots in the chaperones and to counteract their autoinhibitory conformation. This regulatory mechanism of protein activity is evolutionarily conserved among several TSS systems and presents a lucid example of functional advantage conferred upon a biological system by finely tuned structural instability.
Structural instability tuning as a regulatory mechanism in protein-protein interactions.,Chen L, Balabanidou V, Remeta DP, Minetti CA, Portaliou AG, Economou A, Kalodimos CG Mol Cell. 2011 Dec 9;44(5):734-44. PMID:22152477[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen L, Balabanidou V, Remeta DP, Minetti CA, Portaliou AG, Economou A, Kalodimos CG. Structural instability tuning as a regulatory mechanism in protein-protein interactions. Mol Cell. 2011 Dec 9;44(5):734-44. PMID:22152477 doi:10.1016/j.molcel.2011.09.022
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