8f0a

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m (Protected "8f0a" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 8f0a is ON HOLD
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==Client-bound structure of a DegP trimer within a 12mer cage==
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<StructureSection load='8f0a' size='340' side='right'caption='[[8f0a]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8f0a]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F0A 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]] 2.6&#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=8f0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f0a OCA], [https://pdbe.org/8f0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f0a RCSB], [https://www.ebi.ac.uk/pdbsum/8f0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f0a ProSAT]</span></td></tr>
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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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Authors: Harkness, R.W., Ripstein, Z.A., Di Trani, J.M., Kay, L.E.
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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Description: Client-bound structure of a DegP trimer within a 12mer cage
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Kay, L.E]]
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__TOC__
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[[Category: Ripstein, Z.A]]
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</StructureSection>
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[[Category: Harkness, R.W]]
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[[Category: Escherichia coli K-12]]
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[[Category: Di Trani, J.M]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Di Trani JM]]
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[[Category: Harkness RW]]
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[[Category: Kay LE]]
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[[Category: Ripstein ZA]]

Current revision

Client-bound structure of a DegP trimer within a 12mer cage

PDB ID 8f0a

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