3cs0: Difference between revisions

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<StructureSection load='3cs0' size='340' side='right'caption='[[3cs0]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3cs0' size='340' side='right'caption='[[3cs0]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3cs0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CS0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CS0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3cs0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CS0 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">degP, htrA, ptd, b0161, JW0157 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">degP, htrA, ptd, b0161, JW0157 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cs0 OCA], [http://pdbe.org/3cs0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cs0 RCSB], [http://www.ebi.ac.uk/pdbsum/3cs0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cs0 ProSAT]</span></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=3cs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cs0 OCA], [https://pdbe.org/3cs0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cs0 RCSB], [https://www.ebi.ac.uk/pdbsum/3cs0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cs0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>   
[[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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