2l8y

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[[Image:2l8y.png|left|200px]]
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==Solution structure of the E. coli outer membrane protein RcsF (periplasmatic domain)==
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<StructureSection load='2l8y' size='340' side='right' caption='[[2l8y]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
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== Structural highlights ==
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[[2l8y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8Y OCA]. <br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Publication Abstract from PubMed ==
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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>
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The line below this paragraph, containing "STRUCTURE_2l8y", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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{{STRUCTURE_2l8y| PDB=2l8y | SCENE= }}
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===Solution structure of the E. coli outer membrane protein RcsF (periplasmatic domain)===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_21471196}}, adds the Publication Abstract to the page
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 21471196 is the PubMed ID number.
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{{ABSTRACT_PUBMED_21471196}}
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==About this Structure==
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[[2l8y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8Y OCA].
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==Reference==
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<ref group="xtra">PMID:021471196</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Bernhard, F.]]
[[Category: Bernhard, F.]]

Revision as of 08:27, 30 April 2014

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

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