Catabolite control protein: Difference between revisions

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<StructureSection load='2fep' size='350' side='right' caption='Structure of catabolite control protein (grey) complex with Hpr (khaki) and sulfate (PDB entry [[2fep]])' scene=''>
<StructureSection load='2fep' size='350' side='right' caption='Structure of catabolite control protein (blue) complex with Hpr (green) and sulfate (PDB entry [[2fep]])' scene='57/570565/Cv/1'>
== Function ==
    
    
'''Catabolite control protein''' (CcpA) is a regulator of carbon metabolism in gram-positive bacteria.  When high concentrations of glucose-6 phosphate or fructose-1,6-diphosphate are present in the cell, they phosphorylate proteins Hpr or Crh which interact with CcpA.  The latter binds to DNA operator to modulate transcription.  
'''Catabolite control protein''' (CcpA) or '''glucose-resistant amylase regulator''' is a regulator of carbon metabolism in gram-positive bacteria.  When high concentrations of glucose-6 phosphate or fructose-1,6-diphosphate are present in the cell, they phosphorylate proteins HPr or Crh which interact with CcpA.  The latter binds to DNA operator to modulate transcription.<ref>PMID:16321938</ref>
*'''CcpC''' Regulates the transcription of genes belonging to the TCA cycle<ref>PMID:34645869</ref> .
*'''CcpE''' Regulates the transcription of genes belonging to the TCA cycle in ''Staphylococcus aureus''<ref>PMID:25193664</ref> .


==3D structures of catabolite control protein==
== Structural highlights ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
CcpA phosphorylation activity is carried out by a <scene name='57/570565/Cv/2'>phosphorylated Ser residue</scene> (PDB entry [[2fep]]).<ref>PMID:8195089</ref> <ref>PMID:8596444</ref>


[[2jcg]], [[2hsg]] - BmCcpA – ''Bacillus megaterium'' <br />
==3D structures of catabolite control protein==
[[1sxg]], [[1sxh]], [[1sxi]] – BmCcpA (mutant)  <br />
[[Catabolite control protein 3D structures]]
[[2o20]] - CcpA (mutant) – ''Streptococcus lactis'' <br />
 
===CcpA binary complex===
 
[[2oen]] - BmCcpA + phosphocarrier protein Hpr  <br />
[[2fep]] - BsCcpA + phosphocarrier protein Hpr – ''Bacillus subtilis''<br />
 
===CcpA ternary complex===


[[1rzr]] – BmCcpA + phosphocarrier protein Hpr + DNA  <br />
</StructureSection>
[[2nzu]] - BmCcpA + phosphocarrier protein Hpr + glucose-6-phosphate  <br />
[[2nzv]] - BmCcpA + phosphocarrier protein Hpr + fructose-1,6-diphosphate  <br />
[[1zvv]] – BsCcpA + catabolite repression Crh + DNA  <br />
[[3oqm]], [[3oqn]], [[3oqo]] - BsCcpA + phosphocarrier protein Hpr + DNA<br />


== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:03, 15 January 2025

Function

Catabolite control protein (CcpA) or glucose-resistant amylase regulator is a regulator of carbon metabolism in gram-positive bacteria. When high concentrations of glucose-6 phosphate or fructose-1,6-diphosphate are present in the cell, they phosphorylate proteins HPr or Crh which interact with CcpA. The latter binds to DNA operator to modulate transcription.[1]

  • CcpC Regulates the transcription of genes belonging to the TCA cycle[2] .
  • CcpE Regulates the transcription of genes belonging to the TCA cycle in Staphylococcus aureus[3] .

Structural highlights

CcpA phosphorylation activity is carried out by a (PDB entry 2fep).[4] [5]

3D structures of catabolite control protein

Catabolite control protein 3D structures


Structure of catabolite control protein (blue) complex with Hpr (green) and sulfate (PDB entry 2fep)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Iyer R, Baliga NS, Camilli A. Catabolite control protein A (CcpA) contributes to virulence and regulation of sugar metabolism in Streptococcus pneumoniae. J Bacteriol. 2005 Dec;187(24):8340-9. PMID:16321938 doi:http://dx.doi.org/10.1128/JB.187.24.8340-8349.2005
  2. Liu W, Chen J, Jin L, Liu ZY, Lu M, Jiang G, Yang Q, Quan C, Nam KH, Xu Y. Functional and structural analysis of catabolite control protein C that responds to citrate. Sci Rep. 2021 Oct 13;11(1):20285. PMID:34645869 doi:10.1038/s41598-021-99552-x
  3. Hartmann T, Baronian G, Nippe N, Voss M, Schulthess B, Wolz C, Eisenbeis J, Schmidt-Hohagen K, Gaupp R, Sunderkötter C, Beisswenger C, Bals R, Somerville GA, Herrmann M, Molle V, Bischoff M. The catabolite control protein E (CcpE) affects virulence determinant production and pathogenesis of Staphylococcus aureus. J Biol Chem. 2014 Oct 24;289(43):29701-11. PMID:25193664 doi:10.1074/jbc.M114.584979
  4. Deutscher J, Reizer J, Fischer C, Galinier A, Saier MH Jr, Steinmetz M. Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J Bacteriol. 1994 Jun;176(11):3336-44. PMID:8195089
  5. Fujita Y, Miwa Y, Galinier A, Deutscher J. Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr. Mol Microbiol. 1995 Sep;17(5):953-60. PMID:8596444

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Michal Harel, Alexander Berchansky