Catabolite control protein: Difference between revisions
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<StructureSection load='2fep' size='350' side='right' caption='Structure of catabolite control protein ( | <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 | '''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> . | |||
== | == Structural highlights == | ||
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> | |||
==3D structures of catabolite control protein== | |||
[[Catabolite control protein 3D structures]] | |||
== | |||
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</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Latest revision as of 12:03, 15 January 2025
FunctionCatabolite 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]
Structural highlightsCcpA phosphorylation activity is carried out by a (PDB entry 2fep).[4] [5] 3D structures of catabolite control proteinCatabolite control protein 3D structures
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ReferencesReferences
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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