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| | ==Crystal Structure of E. coli YbbN== | | ==Crystal Structure of E. coli YbbN== |
| - | <StructureSection load='3qou' size='340' side='right' caption='[[3qou]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3qou' size='340' side='right'caption='[[3qou]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qou]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QOU FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YbbN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qou OCA], [http://pdbe.org/3qou PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qou RCSB], [http://www.ebi.ac.uk/pdbsum/3qou PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qou ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [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> |
| - | Many proteins contain a thioredoxin (Trx)-like domain fused with one or more partner domains that diversify protein function by the modular construction of new molecules. The Escherichia coli protein YbbN is a Trx-like protein that contains a C-terminal domain with low homology to tetratricopeptide repeat motifs. YbbN has been proposed to act as a chaperone or co-chaperone that aids in heat stress response and DNA synthesis. We report the crystal structure of YbbN, which is an elongated molecule with a mobile Trx domain and four atypical tetratricopeptide repeat motifs. The Trx domain lacks a canonical CXXC active site architecture and is not a functional oxidoreductase. A variety of proteins in E. coli interact with YbbN, including multiple ribosomal protein subunits and a strong interaction with GroEL. YbbN acts as a mild inhibitor of GroESL chaperonin function and ATPase activity, suggesting that it is a negative regulator of the GroESL system. Combined with previous observations that YbbN enhances the DnaK-DnaJ-GrpE chaperone system, we propose that YbbN coordinately regulates the activities of these two prokaryotic chaperones, thereby helping to direct client protein traffic initially to DnaK. Therefore, YbbN may play a role in integrating the activities of different chaperone pathways in E. coli and related bacteria.
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| - | Escherichia coli Thioredoxin-like Protein YbbN Contains an Atypical Tetratricopeptide Repeat Motif and Is a Negative Regulator of GroEL.,Lin J, Wilson MA J Biol Chem. 2011 Jun 3;286(22):19459-69. Epub 2011 Apr 15. PMID:21498507<ref>PMID:21498507</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div> | + | |
| - | <div class="pdbe-citations 3qou" style="background-color:#fffaf0;"></div> | + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Lin, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Wilson, M A]] | + | [[Category: Lin J]] |
| - | [[Category: Lysine dimethylation]] | + | [[Category: Wilson MA]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Tetratricopeptide repeat]]
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| - | [[Category: Thioredoxin-like fold]]
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| Structural highlights
Function
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).[1] [2] [3] [4]
References
- ↑ Caldas T, Malki A, Kern R, Abdallah J, Richarme G. The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase. Biochem Biophys Res Commun. 2006 May 12;343(3):780-6. PMID:16563353 doi:10.1016/j.bbrc.2006.03.028
- ↑ Kthiri F, Le HT, Tagourti J, Kern R, Malki A, Caldas T, Abdallah J, Landoulsi A, Richarme G. The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase. Biochem Biophys Res Commun. 2008 Oct 3;374(4):668-72. PMID:18657513 doi:10.1016/j.bbrc.2008.07.080
- ↑ Lin J, Wilson MA. Escherichia coli Thioredoxin-like Protein YbbN Contains an Atypical Tetratricopeptide Repeat Motif and Is a Negative Regulator of GroEL. J Biol Chem. 2011 Jun 3;286(22):19459-69. Epub 2011 Apr 15. PMID:21498507 doi:10.1074/jbc.M111.238741
- ↑ Goemans CV, Vertommen D, Agrebi R, Collet JF. CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation. Mol Cell. 2018 May 17;70(4):614-627.e7. PMID:29754824 doi:10.1016/j.molcel.2018.04.002
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