3mh4: Difference between revisions
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==HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues== | ==HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues== | ||
<StructureSection load='3mh4' size='340' side='right' caption='[[3mh4]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='3mh4' size='340' side='right'caption='[[3mh4]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mh4]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3mh4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MH4 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">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</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=3mh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mh4 OCA], [https://pdbe.org/3mh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mh4 RCSB], [https://www.ebi.ac.uk/pdbsum/3mh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mh4 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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 3mh4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3mh4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Clausen | [[Category: Large Structures]] | ||
[[Category: Huber | [[Category: Clausen T]] | ||
[[Category: Krojer | [[Category: Huber R]] | ||
[[Category: Sawa | [[Category: Krojer T]] | ||
[[Category: Sawa J]] | |||
