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4a8c

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Revision as of 07:51, 18 August 2022

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

4a8c, resolution 7.50Å

Structural highlights

4a8c is a 12 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4a8a, 4a8b, 4a9g
Activity:	Peptidase Do, with EC number 3.4.21.107
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Waller PR, Sauer RT. Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J Bacteriol. 1996 Feb;178(4):1146-53. PMID:8576051
↑ Kolmar H, Waller PR, Sauer RT. The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation. J Bacteriol. 1996 Oct;178(20):5925-9. PMID:8830688
↑ Malet H, Canellas F, Sawa J, Yan J, Thalassinos K, Ehrmann M, Clausen T, Saibil HR. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nat Struct Mol Biol. 2012 Jan 15;19(2):152-7. doi: 10.1038/nsmb.2210. PMID:22245966 doi:10.1038/nsmb.2210

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4a8c"

@@ Line 3: / Line 3: @@
 <SX load='4a8c' size='340' side='right' viewer='molstar' caption='[[4a8c]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4a8c]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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://proteopedia.org/fgij/fg.htm?mol=4A8C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4a8c]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. 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>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a8a|4a8a]], [[4a8b|4a8b]], [[4a9g|4a9g]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4a8a|4a8a]], [[4a8b|4a8b]], [[4a9g|4a9g]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4a8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a8c OCA], [http://pdbe.org/4a8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a8c RCSB], [http://www.ebi.ac.uk/pdbsum/4a8c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a8c ProSAT]</span></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=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>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==

4a8c

From Proteopedia

Revision as of 07:51, 18 August 2022

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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