4a8d

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[[Image:4a8d.png|left|200px]]
 
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==DegP dodecamer with bound OMP==
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The line below this paragraph, containing "STRUCTURE_4a8d", creates the "Structure Box" on the page.
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<SX load='4a8d' size='340' side='right' viewer='molstar' caption='[[4a8d]], [[Resolution|resolution]] 28.00&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[4a8d]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A8D FirstGlance]. <br>
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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]] 28&#8491;</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=4a8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a8d OCA], [https://pdbe.org/4a8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a8d RCSB], [https://www.ebi.ac.uk/pdbsum/4a8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a8d ProSAT]</span></td></tr>
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{{STRUCTURE_4a8d| PDB=4a8d | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DEGP_ECOLI DEGP_ECOLI] DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP).<ref>PMID:2180903</ref> <ref>PMID:8830688</ref> <ref>PMID:10319814</ref> <ref>PMID:18505836</ref> <ref>PMID:12730160</ref> <ref>PMID:18496527</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===DegP dodecamer with bound OMP===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4a8d" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_22245966}}, adds the Publication Abstract to the page
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 22245966 is the PubMed ID number.
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*[[Porin 3D structures|Porin 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_22245966}}
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<references/>
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__TOC__
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==About this Structure==
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</SX>
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[[4a8d]] is a 13 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=4A8D OCA].
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==Reference==
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<ref group="xtra">PMID:022245966</ref><ref group="xtra">PMID:018496527</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Hydrolase]]
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[[Category: Large Structures]]
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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: Krojer, T.]]
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[[Category: Krojer T]]
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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: Schafer, E.]]
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[[Category: Schafer E]]
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[[Category: Chaperone]]
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[[Category: Hydrolase-transport protein complex]]
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Current revision

DegP dodecamer with bound OMP

4a8d, resolution 28.00Å

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OCA

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