8f21: Difference between revisions

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New page: '''Unreleased structure''' The entry 8f21 is ON HOLD Authors: Harkness, R.W., Ripstein, Z.A., Di Trani, J.M., Kay, L.E. Description: Structure of a 30mer DegP cage bound to the client ...
 
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'''Unreleased structure'''


The entry 8f21 is ON HOLD
==Structure of a 30mer DegP cage bound to the client protein hTRF1==
<StructureSection load='8f21' size='340' side='right'caption='[[8f21]], [[Resolution|resolution]] 14.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8f21]] 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=8F21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F21 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 14.1&#8491;</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=8f21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f21 OCA], [https://pdbe.org/8f21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f21 RCSB], [https://www.ebi.ac.uk/pdbsum/8f21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f21 ProSAT]</span></td></tr>
</table>
== Function ==
[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>


Authors: Harkness, R.W., Ripstein, Z.A., Di Trani, J.M., Kay, L.E.
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
Description: Structure of a 30mer DegP cage bound to the client protein hTRF1
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Kay, L.E]]
__TOC__
[[Category: Ripstein, Z.A]]
</StructureSection>
[[Category: Harkness, R.W]]
[[Category: Escherichia coli K-12]]
[[Category: Di Trani, J.M]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Di Trani JM]]
[[Category: Harkness RW]]
[[Category: Kay LE]]
[[Category: Ripstein ZA]]

Latest revision as of 08:54, 5 July 2023

Structure of a 30mer DegP cage bound to the client protein hTRF1Structure of a 30mer DegP cage bound to the client protein hTRF1

Structural highlights

8f21 is a 9 chain structure with sequence from Escherichia coli K-12 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 14.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3] [4] [5] [6]

See Also

References

  1. ↑ Lipinska B, Zylicz M, Georgopoulos C. The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J Bacteriol. 1990 Apr;172(4):1791-7. PMID:2180903
  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. ↑ Spiess C, Beil A, Ehrmann M. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell. 1999 Apr 30;97(3):339-47. PMID:10319814
  4. ↑ Krojer T, Pangerl K, Kurt J, Sawa J, Stingl C, Mechtler K, Huber R, Ehrmann M, Clausen T. Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins. Proc Natl Acad Sci U S A. 2008 Jun 3;105(22):7702-7. doi:, 10.1073/pnas.0803392105. Epub 2008 May 27. PMID:18505836 doi:10.1073/pnas.0803392105
  5. ↑ Pan KL, Hsiao HC, Weng CL, Wu MS, Chou CP. Roles of DegP in prevention of protein misfolding in the periplasm upon overexpression of penicillin acylase in Escherichia coli. J Bacteriol. 2003 May;185(10):3020-30. PMID:12730160
  6. ↑ Krojer T, Sawa J, Schafer E, Saibil HR, Ehrmann M, Clausen T. Structural basis for the regulated protease and chaperone function of DegP. Nature. 2008 Jun 12;453(7197):885-90. Epub 2008 May 21. PMID:18496527 doi:10.1038/nature07004

8f21, resolution 14.10Å

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