4a8a: Difference between revisions
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< | ==Asymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozyme== | ||
<SX load='4a8a' size='340' side='right' viewer='molstar' caption='[[4a8a]], [[Resolution|resolution]] 14.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4a8a]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A8A FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 14.2Å</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=4a8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a8a OCA], [https://pdbe.org/4a8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a8a RCSB], [https://www.ebi.ac.uk/pdbsum/4a8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a8a ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[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;"> | |||
== Publication Abstract from PubMed == | |||
The HtrA protein family combines chaperone and protease activities and is essential for protein quality control in many organisms. Whereas the mechanisms underlying the proteolytic function of HtrA proteins are well characterized, their chaperone activity remains poorly understood. Here we describe cryo-EM structures of Escherichia coli DegQ in its 12- and 24-mer states in complex with model substrates, providing a structural model of HtrA chaperone action. Up to six lysozyme substrates bind inside the DegQ 12-mer cage and are visualized in a close-to-native state. An asymmetric reconstruction reveals the binding of a well-ordered lysozyme to four DegQ protomers. DegQ PDZ domains are located adjacent to substrate density and their presence is required for chaperone activity. The substrate-interacting regions appear conserved in 12- and 24-mer cages, suggesting a common mechanism of chaperone function. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4a8a" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
[[Category: Escherichia coli]] | == References == | ||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Canellas | [[Category: Canellas F]] | ||
[[Category: Clausen | [[Category: Clausen T]] | ||
[[Category: Ehrmann | [[Category: Ehrmann M]] | ||
[[Category: Malet | [[Category: Malet H]] | ||
[[Category: Saibil | [[Category: Saibil HR]] | ||
[[Category: Sawa | [[Category: Sawa J]] | ||
[[Category: Thalassinos | [[Category: Thalassinos K]] | ||
[[Category: Yan | [[Category: Yan J]] | ||
Latest revision as of 13:47, 9 May 2024
Asymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozymeAsymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozyme
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