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| | <StructureSection load='1x6j' size='340' side='right'caption='[[1x6j]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1x6j' size='340' side='right'caption='[[1x6j]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1x6j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X6J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1X6J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1x6j]] is a 1 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=1X6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X6J FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1x6i|1x6i]]</div></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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ygfY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1x6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x6j OCA], [https://pdbe.org/1x6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x6j RCSB], [https://www.ebi.ac.uk/pdbsum/1x6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x6j ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1x6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x6j OCA], [http://pdbe.org/1x6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x6j RCSB], [http://www.ebi.ac.uk/pdbsum/1x6j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x6j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CPTB_ECOLI CPTB_ECOLI]] Antitoxin component of a toxin-antitoxin (TA) module. When coexpressed with cognate toxin CptA, the antitoxin neutralizes CptA's toxicity. Has been suggested to be a transcriptional regulator.<ref>PMID:22239607</ref> | + | [https://www.uniprot.org/uniprot/SDHE_ECOLI SDHE_ECOLI] An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins (PubMed:22474332, PubMed:26644464, PubMed:24374335). Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SdhA of SDH (PubMed:24374335, PubMed:26644464, PubMed:22474332). Required for flavinylation of the flavoprotein subunit FdrA of fumarate reductase (FDR) (PubMed:26644464). Binds 2 different sites on the flavoprotein target FrdA (and presumably also SdhA), possibly positioning FAD and protein to facilitate the covalent bond formation; covalent attachment of FAD is not required for SDH or FDR complex enzyme formation (PubMed:26644464). Overexpression of this protein and YgfX (formerly cptA) restores production of prodigiosin antibiotic (Pig) in Serratia strains with deletions of sdhE-ygfX (PubMed:22474332).<ref>PMID:23657679</ref> <ref>PMID:24374335</ref> <ref>PMID:26644464</ref> <ref>PMID:22474332</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Demirkan, E Sarikaya]]
| + | [[Category: Doseeva V]] |
| - | [[Category: Doseeva, V]] | + | [[Category: Galkin A]] |
| - | [[Category: Galkin, A]] | + | [[Category: Herzberg O]] |
| - | [[Category: Herzberg, O]] | + | [[Category: Howard A]] |
| - | [[Category: Howard, A]] | + | [[Category: Krajewski W]] |
| - | [[Category: Krajewski, W]] | + | [[Category: Lim K]] |
| - | [[Category: Lim, K]] | + | [[Category: Pullalarevu S]] |
| - | [[Category: Pullalarevu, S]] | + | [[Category: Sarikaya Demirkan E]] |
| - | [[Category: S2F, Structure 2.Function Project]] | + | |
| - | [[Category: Hypothetical protein]]
| + | |
| - | [[Category: S2f]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structure 2 function project]]
| + | |
| - | [[Category: Transcriptional regulation]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| - | [[Category: Ygfy]]
| + | |
| Structural highlights
Function
SDHE_ECOLI An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins (PubMed:22474332, PubMed:26644464, PubMed:24374335). Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SdhA of SDH (PubMed:24374335, PubMed:26644464, PubMed:22474332). Required for flavinylation of the flavoprotein subunit FdrA of fumarate reductase (FDR) (PubMed:26644464). Binds 2 different sites on the flavoprotein target FrdA (and presumably also SdhA), possibly positioning FAD and protein to facilitate the covalent bond formation; covalent attachment of FAD is not required for SDH or FDR complex enzyme formation (PubMed:26644464). Overexpression of this protein and YgfX (formerly cptA) restores production of prodigiosin antibiotic (Pig) in Serratia strains with deletions of sdhE-ygfX (PubMed:22474332).[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ McNeil MB, Iglesias-Cans MC, Clulow JS, Fineran PC. YgfX (CptA) is a multimeric membrane protein that interacts with the succinate dehydrogenase assembly factor SdhE (YgfY). Microbiology. 2013 Jul;159(Pt 7):1352-65. doi: 10.1099/mic.0.068510-0. Epub 2013 , May 8. PMID:23657679 doi:http://dx.doi.org/10.1099/mic.0.068510-0
- ↑ McNeil MB, Hampton HG, Hards KJ, Watson BN, Cook GM, Fineran PC. The succinate dehydrogenase assembly factor, SdhE, is required for the flavinylation and activation of fumarate reductase in bacteria. FEBS Lett. 2014 Jan 31;588(3):414-21. doi: 10.1016/j.febslet.2013.12.019. Epub, 2013 Dec 25. PMID:24374335 doi:http://dx.doi.org/10.1016/j.febslet.2013.12.019
- ↑ Maklashina E, Rajagukguk S, Starbird CA, McDonald WH, Koganitsky A, Eisenbach M, Iverson TM, Cecchini G. Binding of the Covalent Flavin Assembly Factor to the Flavoprotein Subunit of Complex II. J Biol Chem. 2016 Feb 5;291(6):2904-16. doi: 10.1074/jbc.M115.690396. Epub 2015, Dec 7. PMID:26644464 doi:http://dx.doi.org/10.1074/jbc.M115.690396
- ↑ McNeil MB, Clulow JS, Wilf NM, Salmond GP, Fineran PC. SdhE is a conserved protein required for flavinylation of succinate dehydrogenase in bacteria. J Biol Chem. 2012 May 25;287(22):18418-28. doi: 10.1074/jbc.M111.293803. Epub, 2012 Apr 3. PMID:22474332 doi:http://dx.doi.org/10.1074/jbc.M111.293803
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