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4a8a

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Asymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozyme

4a8a, resolution 14.20Å

Structural highlights

4a8a is a 13 chain structure with sequence from Escherichia coli K-12 and Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 14.2Å
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 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4a8a"

@@ Line 1: / Line 1: @@
 ==Asymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozyme==
-<StructureSection load='4a8a' size='340' side='right' caption='[[4a8a]], [[Resolution|resolution]] 14.20&Aring;' scene=''>
+<SX load='4a8a' size='340' side='right' viewer='molstar' caption='[[4a8a]], [[Resolution|resolution]] 14.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4a8a]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A8A FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kxx|1kxx]], [[2ybi|2ybi]], [[1t6v|1t6v]], [[1vds|1vds]], [[1kir|1kir]], [[1yil|1yil]], [[1heo|1heo]], [[1ior|1ior]], [[1ljg|1ljg]], [[1jis|1jis]], [[2w1m|2w1m]], [[1uic|1uic]], [[1ykz|1ykz]], [[1xgq|1xgq]], [[2war|2war]], [[1lj3|1lj3]], [[1dpw|1dpw]], [[8lyz|8lyz]], [[2lyo|2lyo]], [[1g7h|1g7h]], [[1lks|1lks]], [[5lyt|5lyt]], [[1sfb|1sfb]], [[1ir7|1ir7]], [[1xei|1xei]], [[1hel|1hel]], [[1ljf|1ljf]], [[1f10|1f10]], [[1ljk|1ljk]], [[6lyt|6lyt]], [[1zmy|1zmy]], [[2d91|2d91]], [[2xth|2xth]], [[1lze|1lze]], [[1aki|1aki]], [[1yik|1yik]], [[2d6b|2d6b]], [[1lpi|1lpi]], [[1ndg|1ndg]], [[1flw|1flw]], [[4lyt|4lyt]], [[1jit|1jit]], [[1lzn|1lzn]], [[1ja2|1ja2]], [[1wtn|1wtn]], [[2fbb|2fbb]], [[2lym|2lym]], [[1lz9|1lz9]], [[1lse|1lse]], [[1lsm|1lsm]], [[3lym|3lym]], [[7lyz|7lyz]], [[1t3p|1t3p]], [[2bly|2bly]], [[1b0d|1b0d]], [[1her|1her]], [[1ioq|1ioq]], [[1nby|1nby]], [[1qio|1qio]], [[1xgp|1xgp]], [[1ps5|1ps5]], [[1gwd|1gwd]], [[1v7t|1v7t]], [[1h6m|1h6m]], [[1dqj|1dqj]], [[2a7d|2a7d]], [[1z55|1z55]], [[2c8p|2c8p]], [[1lsb|1lsb]], [[1flq|1flq]], [[1jj1|1jj1]], [[2ybl|2ybl]], [[1yqv|1yqv]], [[1hsx|1hsx]], [[2cds|2cds]], [[1hf4|1hf4]], [[1uib|1uib]], [[1ir9|1ir9]], [[1rjc|1rjc]], [[1ic4|1ic4]], [[1ljh|1ljh]], [[1xej|1xej]], [[1ja7|1ja7]], [[1mel|1mel]], [[1ri8|1ri8]], [[1c10|1c10]], [[1lyo|1lyo]], [[2xjw|2xjw]], [[1n4f|1n4f]], [[2w1y|2w1y]], [[1g7m|1g7m]], [[1sf7|1sf7]], [[1lsf|1lsf]], [[1fn5|1fn5]], [[2d4j|2d4j]], [[1c08|1c08]], [[3lyz|3lyz]], [[1bvk|1bvk]], [[1uif|1uif]], [[1vau|1vau]], [[1lma|1lma]], [[1hc0|1hc0]], [[1a2y|1a2y]], [[4lzt|4lzt]], [[1gxv|1gxv]], [[1p2c|1p2c]], [[1ic5|1ic5]], [[1ua6|1ua6]], [[1at5|1at5]], [[1vfb|1vfb]], [[1vat|1vat]], [[1lj4|1lj4]], [[1ja4|1ja4]], [[4lym|4lym]], [[1flu|1flu]], [[1bwh|1bwh]], [[2hfm|2hfm]], [[1io5|1io5]], [[2bpu|2bpu]], [[1lzb|1lzb]], [[1lsc|1lsc]], [[1w6z|1w6z]], [[2ybn|2ybn]], [[3lyo|3lyo]], [[4lyo|4lyo]], [[1kip|1kip]], [[1ic7|1ic7]], [[1lzt|1lzt]], [[2xbr|2xbr]], [[1lys|1lys]], [[1bwj|1bwj]], [[1e8l|1e8l]], [[132l|132l]], [[1sfg|1sfg]], [[1kxw|1kxw]], [[2x0a|2x0a]], [[2c8o|2c8o]], [[1g7l|1g7l]], [[1sf4|1sf4]], [[1yl1|1yl1]], [[1h87|1h87]], [[3lyt|3lyt]], [[1iot|1iot]], [[1dpx|1dpx]], [[1v7s|1v7s]], [[1ja6|1ja6]], [[1ir8|1ir8]], [[1uie|1uie]], [[1lji|1lji]], [[1bwi|1bwi]], [[2iff|2iff]], [[1jj0|1jj0]], [[1rfp|1rfp]], [[1jiy|1jiy]], [[1iee|1iee]], [[1xek|1xek]], [[1at6|1at6]], [[2ydg|2ydg]], [[1mlc|1mlc]], [[2b5z|2b5z]], [[193l|193l]], [[1lsz|1lsz]], [[2ybm|2ybm]], [[1sq2|1sq2]], [[2ybh|2ybh]], [[1vdq|1vdq]], [[1lje|1lje]], [[1b2k|1b2k]], [[2ybj|2ybj]], [[9lyz|9lyz]], [[1uia|1uia]], [[1hen|1hen]], [[1xfp|1xfp]], [[1lsd|1lsd]], [[2blx|2blx]], [[6lyz|6lyz]], [[1nbz|1nbz]], [[1lsg|1lsg]], [[3hfm|3hfm]], [[1ved|1ved]], [[1lyz|1lyz]], [[1uuz|1uuz]], [[2xbs|2xbs]], [[2d4i|2d4i]], [[1fdl|1fdl]], [[1gxx|1gxx]], [[1lzh|1lzh]], [[1jj3|1jj3]], [[1yky|1yky]], [[1kiq|1kiq]], [[1heq|1heq]], [[1uih|1uih]], [[2lzh|2lzh]], [[1kxy|1kxy]], [[2w1l|2w1l]], [[1g7j|1g7j]], [[1bhz|1bhz]], [[1wtm|1wtm]], [[1hep|1hep]], [[1jtt|1jtt]], [[1lza|1lza]], [[3zvq|3zvq]], [[1jpo|1jpo]], [[1j1p|1j1p]], [[1ljj|1ljj]], [[1f0w|1f0w]], [[2w1x|2w1x]], [[1lzg|1lzg]], [[1lzc|1lzc]], [[1rcm|1rcm]], [[1uid|1uid]], [[1bgi|1bgi]], [[1lzd|1lzd]], [[1lcn|1lcn]], [[1hew|1hew]], [[2vb1|2vb1]], [[2aub|2aub]], [[1j1x|1j1x]], [[1ios|1ios]], [[2cgi|2cgi]], [[1uc0|1uc0]], [[1azf|1azf]], [[4lyz|4lyz]], [[1gpq|1gpq]], [[2a6u|2a6u]], [[2d4k|2d4k]], [[1bvx|1bvx]], [[1uig|1uig]], [[4a7d|4a7d]], [[1qtk|1qtk]], [[1lkr|1lkr]], [[1hsw|1hsw]], [[1jto|1jto]], [[5lyz|5lyz]], [[3lzt|3lzt]], [[1ndm|1ndm]], [[1sf6|1sf6]], [[2lyz|2lyz]], [[1fly|1fly]], [[1yl0|1yl0]], [[1j1o|1j1o]], [[2lzt|2lzt]], [[1lsy|1lsy]], [[1uco|1uco]], [[5lym|5lym]], [[1lsa|1lsa]], [[1hem|1hem]], [[1f3j|1f3j]], [[2a7f|2a7f]], [[194l|194l]], [[1lz8|1lz8]], [[1ykx|1ykx]], [[1vdt|1vdt]], [[1lsn|1lsn]], [[1g7i|1g7i]], [[1vdp|1vdp]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 14.2&#8491;</td></tr>
-<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>
+<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>
-<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=4a8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a8a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a8a RCSB], [http://www.ebi.ac.uk/pdbsum/4a8a PDBsum]</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 ==
@@ Line 15: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4a8a" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 21: / Line 24: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Escherichia coli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Gallus gallus]]
-[[Category: Hydrolase]]
+[[Category: Large Structures]]
-[[Category: Canellas, F]]
+[[Category: Canellas F]]
-[[Category: Clausen, T]]
+[[Category: Clausen T]]
-[[Category: Ehrmann, M]]
+[[Category: Ehrmann M]]
-[[Category: Malet, H]]
+[[Category: Malet H]]
-[[Category: Saibil, H R]]
+[[Category: Saibil HR]]
-[[Category: Sawa, J]]
+[[Category: Sawa J]]
-[[Category: Thalassinos, K]]
+[[Category: Thalassinos K]]
-[[Category: Yan, J]]
+[[Category: Yan J]]
-[[Category: Chaperone]]
-[[Category: Hydrolase-hydrolase complex]]

4a8a

From Proteopedia

Current revision

Asymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozyme

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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