4a8c: Difference between revisions
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<SX load='4a8c' size='340' side='right' viewer='molstar' caption='[[4a8c]], [[Resolution|resolution]] 7.50Å' scene=''> | <SX load='4a8c' size='340' side='right' viewer='molstar' caption='[[4a8c]], [[Resolution|resolution]] 7.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a8c]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a8c]] is a 12 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=4A8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A8C FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a8a|4a8a]], [[4a8b|4a8b]], [[4a9g|4a9g]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4a8a|4a8a]], [[4a8b|4a8b]], [[4a9g|4a9g]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a8c OCA], [https://pdbe.org/4a8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a8c RCSB], [https://www.ebi.ac.uk/pdbsum/4a8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a8c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/DEGQ_ECOLI DEGQ_ECOLI]] DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.<ref>PMID:8576051</ref> <ref>PMID:8830688</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||