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| | ==Crystal structure of the protease + PDZ1 domain of DegQ from Escherichia coli== | | ==Crystal structure of the protease + PDZ1 domain of DegQ from Escherichia coli== |
| - | <StructureSection load='3stj' size='340' side='right' caption='[[3stj]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='3stj' size='340' side='right'caption='[[3stj]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3stj]] is a 25 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3STJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3STJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3stj]] is a 25 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3STJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3STJ FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sti|3sti]]</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=3stj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3stj OCA], [https://pdbe.org/3stj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3stj RCSB], [https://www.ebi.ac.uk/pdbsum/3stj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3stj ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">degQ, hhoA, b3234, JW3203 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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| - | <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=3stj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3stj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3stj RCSB], [http://www.ebi.ac.uk/pdbsum/3stj PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DEGQ_ECOLI DEGQ_ECOLI]] DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.<ref>PMID:8576051</ref> <ref>PMID:8830688</ref> | + | [https://www.uniprot.org/uniprot/DEGQ_ECOLI DEGQ_ECOLI] DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.<ref>PMID:8576051</ref> <ref>PMID:8830688</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | In order to react on distinct stress situations and to prevent the accumulation of misfolded proteins, all cells employ a number of proteases and chaperones, which together setup an efficient protein quality control system. The functionality of proteins in the cell envelope of E.coli is monitored by the HtrA proteases DegS, DegP and DegQ. In contrast to DegP and DegS, the structure and function of DegQ has not been addressed in detail. Here, we show that substrate binding triggers the conversion of the resting DegQ hexamer into catalytically active 12- and 24-mers. Interestingly, substrate-induced oligomer reassembly and protease activation depends on the first PDZ domain, but not on the second. Therefore, the regulatory mechanism originally identified in DegP should be a common feature of HtrA proteases, most of which encompass only a single PDZ domain. Using a DegQ mutant lacking the second PDZ domain we determined the high-resolution crystal structure of a dodecameric HtrA complex. The nearly identical domain orientation of protease and PDZ domains within 12- and 24-meric HtrA complexes reveals a conserved PDZ1-->L3-->LD/L1/L2 signaling cascade, in which loop L3 senses the repositioned PDZ1 domain of higher-order, substrate engaged particles and activates protease function. Furthermore, our in vitro and in vivo data imply a pH-related function of DegQ in the bacterial cell envelope.
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| - | Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.,Sawa J, Malet H, Krojer T, Canellas F, Ehrmann M, Clausen T J Biol Chem. 2011 Jun 17. PMID:21685389<ref>PMID:21685389</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Canellas, F]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Clausen, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Ehrmann, M]] | + | [[Category: Canellas F]] |
| - | [[Category: Krojer, T]] | + | [[Category: Clausen T]] |
| - | [[Category: Malet, H]] | + | [[Category: Ehrmann M]] |
| - | [[Category: Sawa, J]] | + | [[Category: Krojer T]] |
| - | [[Category: Chaperone]] | + | [[Category: Malet H]] |
| - | [[Category: Degp]] | + | [[Category: Sawa J]] |
| - | [[Category: Degq]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Pdz domain]]
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| - | [[Category: Protease]]
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| - | [[Category: Serine protease]]
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