2l8y
From Proteopedia
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==Solution structure of the E. coli outer membrane protein RcsF (periplasmatic domain)== | ==Solution structure of the E. coli outer membrane protein RcsF (periplasmatic domain)== | ||
| - | <StructureSection load='2l8y' size='340' side='right' caption='[[2l8y | + | <StructureSection load='2l8y' size='340' side='right'caption='[[2l8y]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2l8y]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2l8y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2L8Y FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 models</td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8y OCA], [https://pdbe.org/2l8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l8y RCSB], [https://www.ebi.ac.uk/pdbsum/2l8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l8y ProSAT]</span></td></tr> |
| + | </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;"> | ||
== Publication Abstract from PubMed == | == 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. | 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. | ||
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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<ref>PMID:21471196</ref> | 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<ref>PMID:21471196</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2l8y" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Bernhard F]] |
| - | + | [[Category: Doetsch V]] | |
| - | [[Category: | + | [[Category: Lohr F]] |
| - | [[Category: | + | [[Category: Rogov VV]] |
| - | [[Category: | + | [[Category: Rogova NY]] |
| - | [[Category: | + | |
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Current revision
Solution structure of the E. coli outer membrane protein RcsF (periplasmatic domain)
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