4a8d: Difference between revisions
No edit summary |
No edit summary |
||
(4 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==DegP dodecamer with bound OMP== | ==DegP dodecamer with bound OMP== | ||
< | <SX load='4a8d' size='340' side='right' viewer='molstar' caption='[[4a8d]], [[Resolution|resolution]] 28.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a8d]] is a 13 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a8d]] 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=4A8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A8D FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 28Å</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=4a8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a8d OCA], [https://pdbe.org/4a8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a8d RCSB], [https://www.ebi.ac.uk/pdbsum/4a8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a8d ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Line 21: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Porin|Porin]] | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
*[[Porin 3D structures|Porin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</ | </SX> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Clausen | [[Category: Clausen T]] | ||
[[Category: Ehrmann | [[Category: Ehrmann M]] | ||
[[Category: Krojer | [[Category: Krojer T]] | ||
[[Category: Malet | [[Category: Malet H]] | ||
[[Category: Saibil | [[Category: Saibil HR]] | ||
[[Category: Sawa | [[Category: Sawa J]] | ||
[[Category: Schafer | [[Category: Schafer E]] | ||