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4a9g

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==Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein==
==Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein==
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<StructureSection load='4a9g' size='340' side='right' caption='[[4a9g]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
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<SX load='4a9g' size='340' side='right' viewer='molstar' caption='[[4a9g]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4a9g]] is a 24 chain structure with sequence from [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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a8a|4a8a]], [[4a8b|4a8b]], [[4a8c|4a8c]]</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">Electron Microscopy, [[Resolution|Resolution]] 7.5&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [https://pdbe.org/4a9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [https://www.ebi.ac.uk/pdbsum/4a9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9g ProSAT]</span></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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [http://www.ebi.ac.uk/pdbsum/4a9g PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4a9g" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Hydrolase]]
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[[Category: Large Structures]]
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[[Category: Canellas, F]]
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[[Category: Canellas F]]
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[[Category: Clausen, T]]
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[[Category: Clausen T]]
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[[Category: Ehrmann, M]]
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[[Category: Ehrmann M]]
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[[Category: Malet, H]]
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[[Category: Malet H]]
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[[Category: Saibil, H R]]
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[[Category: Saibil HR]]
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[[Category: Sawa, J]]
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[[Category: Sawa J]]
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[[Category: Thalassinos, K]]
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[[Category: Thalassinos K]]
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[[Category: Yan, J]]
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[[Category: Yan J]]
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[[Category: Chaperone]]
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Current revision

Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein

4a9g, resolution 7.50Å

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