3sti
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3sti is ON HOLD Authors: Sawa, J., Malet, H., Krojer, T., Canellas, F., Ehrmann, M., Clausen, T. Description: crystal structure of the protease dom...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the protease domain of DegQ from Escherichia coli== | |
| - | + | <StructureSection load='3sti' size='340' side='right'caption='[[3sti]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3sti]] is a 3 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=3STI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3STI FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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=3sti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sti OCA], [https://pdbe.org/3sti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sti RCSB], [https://www.ebi.ac.uk/pdbsum/3sti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sti ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Canellas F]] | ||
| + | [[Category: Clausen T]] | ||
| + | [[Category: Ehrmann M]] | ||
| + | [[Category: Krojer T]] | ||
| + | [[Category: Malet H]] | ||
| + | [[Category: Sawa J]] | ||
Current revision
Crystal structure of the protease domain of DegQ from Escherichia coli
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