2oug: Difference between revisions

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{{Seed}}
[[Image:2oug.png|left|200px]]


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==Crystal structure of the RfaH transcription factor at 2.1A resolution==
The line below this paragraph, containing "STRUCTURE_2oug", creates the "Structure Box" on the page.
<StructureSection load='2oug' size='340' side='right'caption='[[2oug]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2oug]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OUG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oug OCA], [https://pdbe.org/2oug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oug RCSB], [https://www.ebi.ac.uk/pdbsum/2oug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oug ProSAT]</span></td></tr>
{{STRUCTURE_2oug| PDB=2oug |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/RFAH_ECOLI RFAH_ECOLI] Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components. RfaH is recruited into a multi-component RNA polymerase complex by the ops element, which is a short conserved DNA sequence located downstream of the main promoter of these operons. Once bound, RfaH suppresses pausing and inhibits Rho-dependent and intrinsic termination at a subset of sites. Termination signals are bypassed, which allows complete synthesis of long RNA chains. Enhances expression of several operons involved in synthesis of lipopolysaccharides, exopolysaccharides, hemolysin, and sex factor. Also negatively controls expression and surface presentation of AG43 and possibly another AG43-independent factor that mediates cell-cell interactions and biofilm formation.<ref>PMID:1584020</ref> <ref>PMID:8606157</ref> <ref>PMID:8951819</ref> <ref>PMID:9171395</ref> <ref>PMID:9426123</ref> <ref>PMID:10660066</ref> <ref>PMID:12007406</ref> <ref>PMID:11983161</ref> <ref>PMID:16452414</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/2oug_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2oug ConSurf].
<div style="clear:both"></div>


===Crystal structure of the RfaH transcription factor at 2.1A resolution===
==See Also==
 
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
 
== References ==
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{{ABSTRACT_PUBMED_17434131}}
 
==About this Structure==
2OUG is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUG OCA].
 
==Reference==
<ref group="xtra">PMID:17434131</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Artsimovitch, I.]]
[[Category: Large Structures]]
[[Category: Svetlov, V.]]
[[Category: Artsimovitch I]]
[[Category: Vassylyev, D G.]]
[[Category: Svetlov V]]
[[Category: Vassylyeva, M N.]]
[[Category: Vassylyev DG]]
[[Category: Transcription elongation]]
[[Category: Vassylyeva MN]]
[[Category: Transcription factor]]
[[Category: Transcription pausing]]
[[Category: Virulence]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:51:16 2009''

Latest revision as of 12:06, 21 February 2024

Crystal structure of the RfaH transcription factor at 2.1A resolutionCrystal structure of the RfaH transcription factor at 2.1A resolution

Structural highlights

2oug is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RFAH_ECOLI Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components. RfaH is recruited into a multi-component RNA polymerase complex by the ops element, which is a short conserved DNA sequence located downstream of the main promoter of these operons. Once bound, RfaH suppresses pausing and inhibits Rho-dependent and intrinsic termination at a subset of sites. Termination signals are bypassed, which allows complete synthesis of long RNA chains. Enhances expression of several operons involved in synthesis of lipopolysaccharides, exopolysaccharides, hemolysin, and sex factor. Also negatively controls expression and surface presentation of AG43 and possibly another AG43-independent factor that mediates cell-cell interactions and biofilm formation.[1] [2] [3] [4] [5] [6] [7] [8] [9]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Bailey MJ, Koronakis V, Schmoll T, Hughes C. Escherichia coli HlyT protein, a transcriptional activator of haemolysin synthesis and secretion, is encoded by the rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genes. Mol Microbiol. 1992 Apr;6(8):1003-12. PMID:1584020
  2. ↑ Leeds JA, Welch RA. RfaH enhances elongation of Escherichia coli hlyCABD mRNA. J Bacteriol. 1996 Apr;178(7):1850-7. PMID:8606157
  3. ↑ Bailey MJ, Hughes C, Koronakis V. Increased distal gene transcription by the elongation factor RfaH, a specialized homologue of NusG. Mol Microbiol. 1996 Nov;22(4):729-37. PMID:8951819
  4. ↑ Leeds JA, Welch RA. Enhancing transcription through the Escherichia coli hemolysin operon, hlyCABD: RfaH and upstream JUMPStart DNA sequences function together via a postinitiation mechanism. J Bacteriol. 1997 Jun;179(11):3519-27. PMID:9171395
  5. ↑ Bailey MJ, Hughes C, Koronakis V. RfaH and the ops element, components of a novel system controlling bacterial transcription elongation. Mol Microbiol. 1997 Dec;26(5):845-51. PMID:9426123
  6. ↑ Bailey MJ, Hughes C, Koronakis V. In vitro recruitment of the RfaH regulatory protein into a specialised transcription complex, directed by the nucleic acid ops element. Mol Gen Genet. 2000 Jan;262(6):1052-9. PMID:10660066
  7. ↑ Artsimovitch I, Landick R. The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand. Cell. 2002 Apr 19;109(2):193-203. PMID:12007406
  8. ↑ Santangelo TJ, Roberts JW. RfaH, a bacterial transcription antiterminator. Mol Cell. 2002 Apr;9(4):698-700. PMID:11983161
  9. ↑ Beloin C, Michaelis K, Lindner K, Landini P, Hacker J, Ghigo JM, Dobrindt U. The transcriptional antiterminator RfaH represses biofilm formation in Escherichia coli. J Bacteriol. 2006 Feb;188(4):1316-31. PMID:16452414 doi:http://dx.doi.org/10.1128/JB.188.4.1316-1331.2006

2oug, resolution 2.10Å

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