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2l8y

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Revision as of 19:49, 1 August 2018

Solution structure of the E. coli outer membrane protein RcsF (periplasmatic domain)

Structural highlights

2l8y is a 1 chain structure with sequence from Ecoli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	rcsF (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

RcsF, a proposed auxiliary regulator of the regulation of capsule synthesis (rcs) phosphorelay system, is a key element for understanding the RcsC-D-A/B signaling cascade, which is responsible for the regulation of more than 100 genes and is involved in cell division, motility, biofilm formation, and virulence. The RcsC-D-A/B system is one of the most complex bacterial signal transduction pathways, consisting of several membrane-bound and soluble proteins. RcsF is a lipoprotein attached to the outer membrane and plays an important role in activating the RcsC-d-A/B pathway. The exact mechanism of activation of the rcs phosphorelay by RcsF, however, remains unknown. We have analyzed the sequence of RcsF and identified three structural elements: 1) an N-terminal membrane-anchored helix (residues 3-13), 2) a loop (residues 14-48), and 3) a C-terminal folded domain (residues 49-134). We have determined the structure of this C-terminal domain and started to investigate its interaction with potential partners. Important features of its structure are two disulfide bridges between Cys-74 and Cys-118 and between Cys-109 and Cys-124. To evaluate the importance of this RcsF disulfide bridge network in vivo, we have examined the ability of the full-length protein and of specific Cys mutants to initiate the rcs signaling cascade. The results indicate that the Cys-74/Cys-118 and the Cys-109/Cys-124 residues correlate pairwise with the activity of RcsF. Interaction studies showed a weak interaction with an RNA hairpin. However, no interaction could be detected with reagents that are believed to activate the rcs phosphorelay, such as lysozyme, glucose, or Zn(2+) ions.

A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RCSF.,Rogov VV, Rogova NY, Bernhard F, Lohr F, Dotsch V J Biol Chem. 2011 May 27;286(21):18775-83. Epub 2011 Apr 6. PMID:21471196^[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
↑ Rogov VV, Rogova NY, Bernhard F, Lohr F, Dotsch V. A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RCSF. J Biol Chem. 2011 May 27;286(21):18775-83. Epub 2011 Apr 6. PMID:21471196 doi:10.1074/jbc.M111.230185

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l8y"

@@ Line 1: / Line 1: @@
 ==Solution structure of the E. coli outer membrane protein RcsF (periplasmatic domain)==
 <StructureSection load='2l8y' size='340' side='right' caption='[[2l8y]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2l8y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L8Y FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rcsF ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8y OCA], [http://pdbe.org/2l8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l8y RCSB], [http://www.ebi.ac.uk/pdbsum/2l8y PDBsum]</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=2l8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8y OCA], [http://pdbe.org/2l8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l8y RCSB], [http://www.ebi.ac.uk/pdbsum/2l8y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l8y ProSAT]</span></td></tr>
 </table>
 == Function ==

2l8y

From Proteopedia

Revision as of 19:49, 1 August 2018

Solution structure of the E. coli outer membrane protein RcsF (periplasmatic domain)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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