4a8a: Difference between revisions

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

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
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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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]

[2]

[3]

@@ Line 3: / Line 3: @@
 <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 [https://en.wikipedia.org/wiki/Ecoli Ecoli] 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>
+<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"><div style='overflow: auto; max-height: 3em;'>[[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]]</div></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'>[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'>[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>  [[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</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 ==
@@ Line 26: / Line 25: @@
 __TOC__
 </SX>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Peptidase Do]]
+[[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 HR]]
-[[Category: Saibil, H R]]
+[[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: Difference between revisions

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

4a8a: Difference between revisions

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Search