8f26

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m (Protected "8f26" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 8f26 is ON HOLD
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==Structure of a 60mer DegP cage bound to the client protein hTRF1==
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<StructureSection load='8f26' size='340' side='right'caption='[[8f26]], [[Resolution|resolution]] 9.70&Aring;' scene=''>
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Authors: Harkness, R.W., Ripstein, Z.A., Di Trani, J.M., Kay, L.E.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8f26]] is a 3 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=8F26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F26 FirstGlance]. <br>
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Description: Structure of a 60mer DegP cage bound to the client protein hTRF1
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</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=8f26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f26 OCA], [https://pdbe.org/8f26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f26 RCSB], [https://www.ebi.ac.uk/pdbsum/8f26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f26 ProSAT]</span></td></tr>
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[[Category: Unreleased Structures]]
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</table>
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[[Category: Kay, L.E]]
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== Function ==
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[[Category: Ripstein, Z.A]]
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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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[[Category: Harkness, R.W]]
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== References ==
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[[Category: Di Trani, J.M]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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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]]

Revision as of 10:16, 24 November 2022

Structure of a 60mer DegP cage bound to the client protein hTRF1

PDB ID 8f26

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