2fep: Difference between revisions

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==Structure of truncated CcpA in complex with P-Ser-HPr and Sulfate ions==
The line below this paragraph, containing "STRUCTURE_2fep", creates the "Structure Box" on the page.
<StructureSection load='2fep' size='340' side='right'caption='[[2fep]], [[Resolution|resolution]] 2.45&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'>[[2fep]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FEP FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_2fep| PDB=2fep |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fep OCA], [https://pdbe.org/2fep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fep RCSB], [https://www.ebi.ac.uk/pdbsum/2fep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fep ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCPA_BACSU CCPA_BACSU] Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P-Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons.<ref>PMID:1904524</ref> <ref>PMID:7665492</ref> <ref>PMID:10559165</ref> <ref>PMID:11557150</ref> <ref>PMID:21106498</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/fe/2fep_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=2fep ConSurf].
<div style="clear:both"></div>


===Structure of truncated CcpA in complex with P-Ser-HPr and Sulfate ions===
==See Also==
 
*[[Catabolite control protein|Catabolite control protein]]
 
*[[Catabolite control protein 3D structures|Catabolite control protein 3D structures]]
==About this Structure==
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
[[2fep]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEP OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:016755587</ref><references group="xtra"/>
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Chaptal, V.]]
[[Category: Large Structures]]
[[Category: Deutscher, J.]]
[[Category: Chaptal V]]
[[Category: Galinier, A.]]
[[Category: Deutscher J]]
[[Category: Gueguen-Chaignon, V.]]
[[Category: Galinier A]]
[[Category: Lecampion, C.]]
[[Category: Gueguen-Chaignon V]]
[[Category: Meyer, P.]]
[[Category: Lecampion C]]
[[Category: Nessler, S.]]
[[Category: Meyer P]]
[[Category: Poncet, S.]]
[[Category: Nessler S]]
[[Category: Ccpa]]
[[Category: Poncet S]]
[[Category: Hpr]]
[[Category: Transcription]]
[[Category: Transcriptional regulator]]

Latest revision as of 12:25, 30 August 2023

Structure of truncated CcpA in complex with P-Ser-HPr and Sulfate ionsStructure of truncated CcpA in complex with P-Ser-HPr and Sulfate ions

Structural highlights

2fep is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.45Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCPA_BACSU Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P-Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons.[1] [2] [3] [4] [5]

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. ↑ Henkin TM, Grundy FJ, Nicholson WL, Chambliss GH. Catabolite repression of alpha-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacl and galR repressors. Mol Microbiol. 1991 Mar;5(3):575-84. PMID:1904524
  2. ↑ Kim JH, Guvener ZT, Cho JY, Chung KC, Chambliss GH. Specificity of DNA binding activity of the Bacillus subtilis catabolite control protein CcpA. J Bacteriol. 1995 Sep;177(17):5129-34. PMID:7665492
  3. ↑ Tobisch S, Zuhlke D, Bernhardt J, Stulke J, Hecker M. Role of CcpA in regulation of the central pathways of carbon catabolism in Bacillus subtilis. J Bacteriol. 1999 Nov;181(22):6996-7004. PMID:10559165
  4. ↑ Ludwig H, Stulke J. The Bacillus subtilis catabolite control protein CcpA exerts all its regulatory functions by DNA-binding. FEMS Microbiol Lett. 2001 Sep 11;203(1):125-9. PMID:11557150
  5. ↑ Schumacher MA, Sprehe M, Bartholomae M, Hillen W, Brennan RG. Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-affinity binding to degenerate DNA operators. Nucleic Acids Res. 2010 Nov 23. PMID:21106498 doi:10.1093/nar/gkq1177

2fep, resolution 2.45Å

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