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| | <StructureSection load='2y1b' size='340' side='right'caption='[[2y1b]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2y1b' size='340' side='right'caption='[[2y1b]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y1B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y1b]] 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=2Y1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y1B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3C:5-AMINO-2,4,6-TRIIODOBENZENE-1,3-DICARBOXYLIC+ACID'>I3C</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3C:5-AMINO-2,4,6-TRIIODOBENZENE-1,3-DICARBOXYLIC+ACID'>I3C</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2y1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y1b OCA], [https://pdbe.org/2y1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y1b RCSB], [https://www.ebi.ac.uk/pdbsum/2y1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y1b 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=2y1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y1b OCA], [https://pdbe.org/2y1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y1b RCSB], [https://www.ebi.ac.uk/pdbsum/2y1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y1b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/RCSF_ECOLI RCSF_ECOLI] Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.<ref>PMID:13129944</ref> <ref>PMID:14651646</ref> <ref>PMID:16166540</ref> <ref>PMID:16740933</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boujtat, A]] | + | [[Category: Boujtat A]] |
| - | [[Category: Collet, J F]] | + | [[Category: Collet JF]] |
| - | [[Category: Declercq, J P]] | + | [[Category: Declercq JP]] |
| - | [[Category: Leverrier, P]] | + | [[Category: Leverrier P]] |
| - | [[Category: Capsule]]
| + | |
| - | [[Category: Colanic acid]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Mucoidity]]
| + | |
| - | [[Category: Phosphorelay]]
| + | |
| - | [[Category: Rc]]
| + | |
| Structural highlights
Function
RCSF_ECOLI Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.[1] [2] [3] [4]
Publication Abstract from PubMed
The bacterial Rcs phosphorelay is a stress-induced defense mechanism that controls the expression of numerous genes, including those for capsular polysaccharides, motility, and virulence factors. It is a complex multicomponent system that includes the histidine kinase (RcsC) and the response regulator (RcsB) and also auxiliary proteins such as RcsF. RcsF is an outer membrane lipoprotein that transmits signals from the cell surface to RcsC. The physiological signals that activate RcsF and how RcsF interacts with RcsC remain unknown. Here, we report the three-dimensional structure of RcsF. The fold of the protein is characterized by the presence of a central 4-stranded beta sheet, which is conserved in several other proteins, including the copper-binding domain of the amyloid precursor protein. RcsF, which contains four conserved cysteine residues, presents two nonconsecutive disulfides between Cys(74) and Cys(118) and between Cys(109) and Cys(124), respectively. These two disulfides are not functionally equivalent; the Cys(109)-Cys(124) disulfide is particularly important for the assembly of an active RcsF. Moreover, we show that formation of the nonconsecutive disulfides of RcsF depends on the periplasmic disulfide isomerase DsbC. We trapped RcsF in a mixed disulfide complex with DsbC, and we show that deletion of dsbC prevents the activation of the Rcs phosphorelay by signals that function through RcsF. The three-dimensional structure of RcsF provides the structural basis to understand how this protein triggers the Rcs signaling cascade.
Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC.,Leverrier P, Declercq JP, Denoncin K, Vertommen D, Hiniker A, Cho SH, Collet JF J Biol Chem. 2011 May 13;286(19):16734-42. Epub 2011 Mar 16. PMID:21454485[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
- ↑ Ferrieres L, Clarke DJ. The RcsC sensor kinase is required for normal biofilm formation in Escherichia coli K-12 and controls the expression of a regulon in response to growth on a solid surface. Mol Microbiol. 2003 Dec;50(5):1665-82. PMID:14651646
- ↑ Majdalani N, Heck M, Stout V, Gottesman S. Role of RcsF in signaling to the Rcs phosphorelay pathway in Escherichia coli. J Bacteriol. 2005 Oct;187(19):6770-8. PMID:16166540 doi:10.1128/JB.187.19.6770-6778.2005
- ↑ Castanie-Cornet MP, Cam K, Jacq A. RcsF is an outer membrane lipoprotein involved in the RcsCDB phosphorelay signaling pathway in Escherichia coli. J Bacteriol. 2006 Jun;188(12):4264-70. PMID:16740933 doi:http://dx.doi.org/10.1128/JB.00004-06
- ↑ Leverrier P, Declercq JP, Denoncin K, Vertommen D, Hiniker A, Cho SH, Collet JF. Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC. J Biol Chem. 2011 May 13;286(19):16734-42. Epub 2011 Mar 16. PMID:21454485 doi:10.1074/jbc.M111.224865
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