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2zle

From Proteopedia

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(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_2zle", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
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[[Image:2zle.jpg|left|200px]]
 
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==Cryo-EM structure of DegP12/OMP==
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The line below this paragraph, containing "STRUCTURE_2zle", creates the "Structure Box" on the page.
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<SX load='2zle' size='340' side='right' viewer='molstar' caption='[[2zle]], [[Resolution|resolution]] 28.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[2zle]] 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=2ZLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZLE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=2zle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zle OCA], [https://pdbe.org/2zle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zle RCSB], [https://www.ebi.ac.uk/pdbsum/2zle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zle ProSAT]</span></td></tr>
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{{STRUCTURE_2zle| PDB=2zle | 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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zl/2zle_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2zle ConSurf].
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<div style="clear:both"></div>
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'''Cryo-EM structure of DegP12/OMP'''
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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*[[Porin 3D structures|Porin 3D structures]]
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==Overview==
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== References ==
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All organisms have to monitor the folding state of cellular proteins precisely. The heat-shock protein DegP is a protein quality control factor in the bacterial envelope that is involved in eliminating misfolded proteins and in the biogenesis of outer-membrane proteins. Here we describe the molecular mechanisms underlying the regulated protease and chaperone function of DegP from Escherichia coli. We show that binding of misfolded proteins transforms hexameric DegP into large, catalytically active 12-meric and 24-meric multimers. A structural analysis of these particles revealed that DegP represents a protein packaging device whose central compartment is adaptable to the size and concentration of substrate. Moreover, the inner cavity serves antagonistic functions. Whereas the encapsulation of folded protomers of outer-membrane proteins is protective and might allow safe transit through the periplasm, misfolded proteins are eliminated in the molecular reaction chamber. Oligomer reassembly and concomitant activation on substrate binding may also be critical in regulating other HtrA proteases implicated in protein-folding diseases.
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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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2ZLE is a [[Protein complex]] structure of sequences 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=2ZLE OCA].
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==Reference==
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Structural basis for the regulated protease and chaperone function of DegP., Krojer T, Sawa J, Schafer E, Saibil HR, Ehrmann M, Clausen T, Nature. 2008 May 21;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18496527 18496527]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Saibil, H R.]]
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[[Category: Saibil HR]]
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[[Category: Schaefer, E.]]
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[[Category: Schaefer E]]
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[[Category: Chaperone]]
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[[Category: Degp]]
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[[Category: Htra]]
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[[Category: Hydrolase]]
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[[Category: Ion transport]]
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[[Category: Omp]]
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[[Category: Outer membrane protein]]
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[[Category: Pdz]]
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[[Category: Periplasm]]
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[[Category: Phage recognition]]
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[[Category: Porin]]
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[[Category: Protease]]
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[[Category: Serine protease]]
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[[Category: Stress response]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:54:03 2008''
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Current revision

Cryo-EM structure of DegP12/OMP

2zle, resolution 28.00Å

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