3qou
From Proteopedia
(Difference between revisions)
m (Protected "3qou" [edit=sysop:move=sysop]) |
|||
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of E. coli YbbN== | |
| - | + | <StructureSection load='3qou' size='340' side='right'caption='[[3qou]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3qou]] is a 1 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=3QOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QOU 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]] 1.8Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></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=3qou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qou OCA], [https://pdbe.org/3qou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qou RCSB], [https://www.ebi.ac.uk/pdbsum/3qou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qou ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CNOX_ECOLI CNOX_ECOLI] Chaperedoxin that combines a chaperone activity with a redox-protective function (PubMed:16563353, PubMed:18657513, PubMed:29754824). Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation (PubMed:29754824). Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes (PubMed:29754824). After bleach stress, it transfers its substrates to the GroEL/GroES and DnaK/DnaJ/GrpE foldases (PubMed:29754824). Lacks oxidoreductase activity (PubMed:21498507, PubMed:29754824).<ref>PMID:16563353</ref> <ref>PMID:18657513</ref> <ref>PMID:21498507</ref> <ref>PMID:29754824</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lin J]] | ||
| + | [[Category: Wilson MA]] | ||
Current revision
Crystal Structure of E. coli YbbN
| |||||||||||
