3ou0

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[[Image:3ou0.png|left|200px]]
 
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==re-refined 3CS0==
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The line below this paragraph, containing "STRUCTURE_3ou0", creates the "Structure Box" on the page.
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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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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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{{STRUCTURE_3ou0| PDB=3ou0 | SCENE= }}
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein quality control requires careful regulation of intracellular proteolysis. For DegP, a periplasmic protease, substrates promote assembly of inactive hexamers into proteolytically active cages with 12, 18, 24, or 30 subunits. Here, we show that sensitive activation and cage assembly require covalent linkage of distinct substrate sequences that affect degradation (degrons). One degron binds the DegP active site, and another degron binds a separate tethering site in PDZ1 in the crystal structure of a substrate-bound DegP dodecamer. FRET experiments demonstrate that active cages assemble rapidly in a reaction that is positively cooperative in substrate concentration, remain stably assembled while uncleaved substrate is present, and dissociate once degradation is complete. Thus, the energy of binding of linked substrate degrons drives assembly of the proteolytic machine responsible for subsequent degradation. Substrate cleavage and depletion results in disassembly, ensuring that DegP is proteolytically active only when sufficient quantities of protein substrates are present.
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===re-refined 3CS0===
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Covalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic Cages.,Kim S, Grant RA, Sauer RT Cell. 2011 Apr 1;145(1):67-78. PMID:21458668<ref>PMID:21458668</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ou0" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21458668}}, adds the Publication Abstract to the page
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21458668 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21458668}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3ou0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://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].
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==Reference==
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<ref group="xtra">PMID:21458668</ref><ref group="xtra">PMID:18496527</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Grant, R A.]]
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[[Category: Large Structures]]
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[[Category: Kim, S.]]
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[[Category: Grant RA]]
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[[Category: Sauer, R T.]]
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[[Category: Kim S]]
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[[Category: Sauer RT]]

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re-refined 3CS0

PDB ID 3ou0

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