4a8c

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==Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with a binding peptide==
==Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with a binding peptide==
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<StructureSection load='4a8c' size='340' side='right' caption='[[4a8c]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
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<SX load='4a8c' size='340' side='right' viewer='molstar' caption='[[4a8c]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4a8c]] is a 12 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=4A8C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A8C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4a8c]] is a 12 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=4A8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A8C FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a8a|4a8a]], [[4a8b|4a8b]], [[4a9g|4a9g]]</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><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=4a8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a8c OCA], [https://pdbe.org/4a8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a8c RCSB], [https://www.ebi.ac.uk/pdbsum/4a8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a8c ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a8c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a8c RCSB], [http://www.ebi.ac.uk/pdbsum/4a8c PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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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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Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.,Malet H, Canellas F, Sawa J, Yan J, Thalassinos K, Ehrmann M, Clausen T, Saibil HR Nat Struct Mol Biol. 2012 Jan 15;19(2):152-7. doi: 10.1038/nsmb.2210. PMID:22245966<ref>PMID:22245966</ref>
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.,Malet H, Canellas F, Sawa J, Yan J, Thalassinos K, Ehrmann M, Clausen T, Saibil HR Nat Struct Mol Biol. 2012 Jan 15;19(2):152-7. doi: 10.1038/nsmb.2210. PMID:22245966<ref>PMID:22245966</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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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 4a8c" 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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[[Category: Hydrolase]]
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Current revision

Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with a binding peptide

4a8c, resolution 7.50Å

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