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- | [[Image:1ky9.gif|left|200px]] | |
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- | {{Structure
| + | ==Crystal Structure of DegP (HtrA)== |
- | |PDB= 1ky9 |SIZE=350|CAPTION= <scene name='initialview01'>1ky9</scene>, resolution 2.8Å
| + | <StructureSection load='1ky9' size='340' side='right'caption='[[1ky9]], [[Resolution|resolution]] 2.80Å' scene=''> |
- | |SITE=
| + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
| + | <table><tr><td colspan='2'>[[1ky9]] is a 2 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=1KY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KY9 FirstGlance]. <br> |
- | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
- | |GENE= degP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
- | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ky9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky9 OCA], [https://pdbe.org/1ky9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ky9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ky9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ky9 ProSAT]</span></td></tr> |
- | |RELATEDENTRY= | + | </table> |
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ky9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky9 OCA], [http://www.ebi.ac.uk/pdbsum/1ky9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ky9 RCSB]</span>
| + | == 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> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ky/1ky9_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ky9 ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''Crystal Structure of DegP (HtrA)'''
| + | ==See Also== |
- | | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
- | | + | == References == |
- | ==Overview== | + | <references/> |
- | Molecular chaperones and proteases monitor the folded state of other proteins. In addition to recognizing non-native conformations, these quality control factors distinguish substrates that can be refolded from those that need to be degraded. To investigate the molecular basis of this process, we have solved the crystal structure of DegP (also known as HtrA), a widely conserved heat shock protein that combines refolding and proteolytic activities. The DegP hexamer is formed by staggered association of trimeric rings. The proteolytic sites are located in a central cavity that is only accessible laterally. The mobile side-walls are constructed by twelve PDZ domains, which mediate the opening and closing of the particle and probably the initial binding of substrate. The inner cavity is lined by several hydrophobic patches that may act as docking sites for unfolded polypeptides. In the chaperone conformation, the protease domain of DegP exists in an inactive state, in which substrate binding in addition to catalysis is abolished.
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure==
| + | |
- | 1KY9 is a [[Single protein]] structure of 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=1KY9 OCA].
| + | |
- | | + | |
- | ==Reference== | + | |
- | Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine., Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T, Nature. 2002 Mar 28;416(6879):455-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11919638 11919638]
| + | |
| [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
- | [[Category: Single protein]] | + | [[Category: Large Structures]] |
- | [[Category: Clausen, T.]] | + | [[Category: Clausen T]] |
- | [[Category: Ehrmann, M.]] | + | [[Category: Ehrmann M]] |
- | [[Category: Garrido-Franco, M.]] | + | [[Category: Garrido-Franco M]] |
- | [[Category: Huber, R.]] | + | [[Category: Huber R]] |
- | [[Category: Krojer, T.]] | + | [[Category: Krojer T]] |
- | [[Category: atp-independent]]
| + | |
- | [[Category: cage-forming protein]]
| + | |
- | [[Category: chaperone]]
| + | |
- | [[Category: pdz]]
| + | |
- | [[Category: periplasm]]
| + | |
- | [[Category: protein quality control]]
| + | |
- | [[Category: serine protease]]
| + | |
- | [[Category: temperature-regulated]]
| + | |
- | [[Category: trypsin]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:55:25 2008''
| + | |
| Structural highlights
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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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