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| | ==Crystal structure of non-phosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli== | | ==Crystal structure of non-phosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli== |
| - | <StructureSection load='5i4c' size='340' side='right' caption='[[5i4c]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5i4c' size='340' side='right'caption='[[5i4c]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i4c]] 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=5I4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I4C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i4c]] 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=5I4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I4C FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rcsB, b2217, JW2205 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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='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=5i4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i4c OCA], [http://pdbe.org/5i4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i4c RCSB], [http://www.ebi.ac.uk/pdbsum/5i4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i4c ProSAT]</span></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=5i4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i4c OCA], [https://pdbe.org/5i4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i4c RCSB], [https://www.ebi.ac.uk/pdbsum/5i4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i4c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RCSB_ECOLI RCSB_ECOLI]] Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. The system regulates expression of numerous genes, including genes involved in colanic acid capsule synthesis, biofilm formation, cell division and outer membrane proteins synthesis. Also involved, with GadE, in control of glutamate-dependent acid resistance, and, with BglJ, in derepression of the cryptic bgl operon. The RcsB-BglJ activity is probably independent of RcsB phosphorylation.[HAMAP-Rule:MF_00981]<ref>PMID:10702265</ref> <ref>PMID:11309126</ref> <ref>PMID:11566985</ref> <ref>PMID:13129944</ref> <ref>PMID:1597415</ref> <ref>PMID:20189963</ref> <ref>PMID:20952573</ref> | + | [https://www.uniprot.org/uniprot/RCSB_ECOLI RCSB_ECOLI] Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. The system regulates expression of numerous genes, including genes involved in colanic acid capsule synthesis, biofilm formation, cell division and outer membrane proteins synthesis. Also involved, with GadE, in control of glutamate-dependent acid resistance, and, with BglJ, in derepression of the cryptic bgl operon. The RcsB-BglJ activity is probably independent of RcsB phosphorylation.[HAMAP-Rule:MF_00981]<ref>PMID:10702265</ref> <ref>PMID:11309126</ref> <ref>PMID:11566985</ref> <ref>PMID:13129944</ref> <ref>PMID:1597415</ref> <ref>PMID:20189963</ref> <ref>PMID:20952573</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5i4c" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5i4c" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Response regulator 3D structure|Response regulator 3D structure]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Anderson, W F]] | + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | + | [[Category: Anderson WF]] |
| - | [[Category: Filippova, E V]] | + | [[Category: Filippova EV]] |
| - | [[Category: Minasov, G]] | + | [[Category: Minasov G]] |
| - | [[Category: Pshenychnyi, S]] | + | [[Category: Pshenychnyi S]] |
| - | [[Category: Ruan, J]] | + | [[Category: Ruan J]] |
| - | [[Category: Wawrzak, Z]] | + | [[Category: Wawrzak Z]] |
| - | [[Category: Wolfe, A J]] | + | [[Category: Wolfe AJ]] |
| - | [[Category: Csgid]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Rcs phosphorelay]]
| + | |
| - | [[Category: Rpra]]
| + | |
| - | [[Category: Transcriptional regulator]]
| + | |
| Structural highlights
Function
RCSB_ECOLI Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. The system regulates expression of numerous genes, including genes involved in colanic acid capsule synthesis, biofilm formation, cell division and outer membrane proteins synthesis. Also involved, with GadE, in control of glutamate-dependent acid resistance, and, with BglJ, in derepression of the cryptic bgl operon. The RcsB-BglJ activity is probably independent of RcsB phosphorylation.[HAMAP-Rule:MF_00981][1] [2] [3] [4] [5] [6] [7]
Publication Abstract from PubMed
RcsB, the transcription-associated response regulator of the Rcs phosphorelay two-component signal transduction system, activates cell stress responses associated with desiccation, cell wall biosynthesis, cell division, virulence, biofilm formation and antibiotic resistance in enteric bacterial pathogens. RcsB belongs to the FixJ/NarL family of transcriptional regulators, which are characterized by a highly conserved C-terminal DNA-binding domain. The N-terminal domain of RcsB belongs to the family of two-component receiver domains. This receiver domain contains the phosphoacceptor site and participates in RcsB dimer formation; it also contributes to dimer formation with other transcription factor partners. Here, we describe the crystal structure of the Escherichia coli RcsB receiver domain in its non-phosphorylated state. The structure reveals important molecular details of phosphorylation-independent dimerization of RcsB and has implication for the formation of heterodimers. This article is protected by copyright. All rights reserved.
Crystal structure of non-phosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli.,Filippova EV, Wawrzak Z, Ruan J, Pshenychnyi S, Schultz RM, Wolfe AJ, Anderson WF Protein Sci. 2016 Sep 27. doi: 10.1002/pro.3050. PMID:27670836[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wehland M, Bernhard F. The RcsAB box. Characterization of a new operator essential for the regulation of exopolysaccharide biosynthesis in enteric bacteria. J Biol Chem. 2000 Mar 10;275(10):7013-20. PMID:10702265
- ↑ Takeda S, Fujisawa Y, Matsubara M, Aiba H, Mizuno T. A novel feature of the multistep phosphorelay in Escherichia coli: a revised model of the RcsC --> YojN --> RcsB signalling pathway implicated in capsular synthesis and swarming behaviour. Mol Microbiol. 2001 Apr;40(2):440-50. PMID:11309126
- ↑ Davalos-Garcia M, Conter A, Toesca I, Gutierrez C, Cam K. Regulation of osmC gene expression by the two-component system rcsB-rcsC in Escherichia coli. J Bacteriol. 2001 Oct;183(20):5870-6. PMID:11566985 doi:http://dx.doi.org/10.1128/JB.***********-5876.2001
- ↑ Hagiwara D, Sugiura M, Oshima T, Mori H, Aiba H, Yamashino T, Mizuno T. Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli. J Bacteriol. 2003 Oct;185(19):5735-46. PMID:13129944
- ↑ Gervais FG, Phoenix P, Drapeau GR. The rcsB gene, a positive regulator of colanic acid biosynthesis in Escherichia coli, is also an activator of ftsZ expression. J Bacteriol. 1992 Jun;174(12):3964-71. PMID:1597415
- ↑ Castanie-Cornet MP, Cam K, Bastiat B, Cros A, Bordes P, Gutierrez C. Acid stress response in Escherichia coli: mechanism of regulation of gadA transcription by RcsB and GadE. Nucleic Acids Res. 2010 Jun;38(11):3546-54. doi: 10.1093/nar/gkq097. Epub 2010, Feb 26. PMID:20189963 doi:http://dx.doi.org/10.1093/nar/gkq097
- ↑ Venkatesh GR, Kembou Koungni FC, Paukner A, Stratmann T, Blissenbach B, Schnetz K. BglJ-RcsB heterodimers relieve repression of the Escherichia coli bgl operon by H-NS. J Bacteriol. 2010 Dec;192(24):6456-64. doi: 10.1128/JB.00807-10. Epub 2010 Oct, 15. PMID:20952573 doi:http://dx.doi.org/10.1128/JB.00807-10
- ↑ Filippova EV, Wawrzak Z, Ruan J, Pshenychnyi S, Schultz RM, Wolfe AJ, Anderson WF. Crystal structure of non-phosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli. Protein Sci. 2016 Sep 27. doi: 10.1002/pro.3050. PMID:27670836 doi:http://dx.doi.org/10.1002/pro.3050
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