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3ou0

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(New page: '''Unreleased structure''' The entry 3ou0 is ON HOLD Authors: Sauer, R.T., Grant, R.A., Kim, S. Description: re-refined 3CS0 ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on W...)
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'''Unreleased structure'''
 
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The entry 3ou0 is ON HOLD
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==re-refined 3CS0==
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<StructureSection load='3ou0' size='340' side='right'caption='[[3ou0]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ou0]] is a 3 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=3OU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OU0 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">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<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>
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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=3ou0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ou0 OCA], [https://pdbe.org/3ou0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ou0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ou0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ou0 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: Sauer, R.T., Grant, R.A., Kim, S.
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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Description: re-refined 3CS0
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== References ==
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<references/>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 14:34:58 2010''
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Grant RA]]
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[[Category: Kim S]]
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[[Category: Sauer RT]]

Current revision

re-refined 3CS0

PDB ID 3ou0

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