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词条 Catabolite Control Protein A
释义

  1. Structure

  2. References

Catabolite Control Protein A (CcpA) is a master regulator of carbon metabolism in gram-positive bacteria.[2] It is a member of the LacI/GalR transcription regulator family.[2] In contrast to most LacI/GalR proteins, CcpA is allosterically regulated principally by a protein-protein interaction, rather than a protein-small molecule interaction.[2] CcpA interacts with the phosphorylated form of Hpr[1] and Crh,[3] which is formed when high concentrations of glucose or fructose-1,6-bisphosphate[3] are present in the cell. Interaction of Hpr or Crh modulates the DNA sequence specificity of CcpA, allowing it to bind operator DNA to modulate transcription.[2] Small molecules glucose-6-phosphate and fructose-1,6-bisphosphate are also known allosteric effectors, fine-tuning CcpA function.[4]

Structure

The DNA-binding functional unit of CcpA consists of a homodimer.[2] The N-terminal region of each monomer form a DNA-binding site while the C-terminal portion forms a "regulatory" domain. A short linker connects the N-terminal DNA binding domain and the C-terminal regulatory domain, which partially contacts DNA when bound.[2] The LacI/GalR subfamily can be functionally subdivided based on the presence or absence of a "YxxPxxxAxxL" motif in the liker sequence; CcpA belongs to the subdivision containing this motif.[5] The regulatory domain is further subdivided into a N-terminal and C-terminal subdomain. Small molecule effector binding occurs in the cleft between these subdomains.[4] Binding to phosphorylated Hpr/Crh occurs along the regulatory domain's N-subdomain.[1]

References

1. ^1 2 {{Cite journal | last1 = Schumacher | first1 = M. A. | last2 = Allen | first2 = G. S. | last3 = Diel | first3 = M. | last4 = Seidel | first4 = G. | last5 = Hillen | first5 = W. | last6 = Brennan | first6 = R. G. | doi = 10.1016/j.cell.2004.08.027 | title = Structural Basis for Allosteric Control of the Transcription Regulator CcpA by the Phosphoprotein HPr-Ser46-P | journal = Cell | volume = 118 | issue = 6 | pages = 731–741 | year = 2004 | pmid = 15369672 | pmc = }}
2. ^1 2 3 4 5 {{Cite journal | last1 = Swint-Kruse | first1 = L. | last2 = Matthews | first2 = K. S. | doi = 10.1016/j.mib.2009.01.009 | title = Allostery in the LacI/GalR Family: Variations on a Theme | journal = Current Opinion in Microbiology | volume = 12 | issue = 2 | pages = 129–137 | year = 2009 | pmid = 19269243 | pmc =2688824 }}
3. ^1 {{Cite journal | last1 = Landmann | first1 = J. J. | last2 = Busse | first2 = R. A. | last3 = Latz | first3 = J. H. | last4 = Singh | first4 = K. D. | last5 = Stülke | first5 = J. R. | last6 = Görke | first6 = B. | doi = 10.1111/j.1365-2958.2011.07857.x | title = Crh, the paralogue of the phosphocarrier protein HPr, controls the methylglyoxal bypass of glycolysis in Bacillus subtilis | journal = Molecular Microbiology | volume = 82 | issue = 3 | pages = 770–787 | year = 2011 | pmid = 21992469 | pmc = }}
4. ^1 {{Cite journal | last1 = Schumacher | first1 = M. A. | last2 = Seidel | first2 = G. | last3 = Hillen | first3 = W. | last4 = Brennan | first4 = R. G. | title = Structural Mechanism for the Fine-tuning of CcpA Function by the Small Molecule Effectors Glucose 6-Phosphate and Fructose 1,6-Bisphosphate | doi = 10.1016/j.jmb.2007.02.054 | journal = Journal of Molecular Biology | volume = 368 | issue = 4 | pages = 1042–1050 | year = 2007 | pmid = 17376479 | pmc = }}
5. ^{{Cite journal | last1 = Tungtur | first1 = S. | last2 = Parente | first2 = D. J. | last3 = Swint-Kruse | first3 = L. | doi = 10.1002/prot.22985 | title = Functionally important positions can comprise the majority of a protein's architecture | journal = Proteins: Structure, Function, and Bioinformatics | volume = 79 | issue = 5 | pages = 1589–1608 | year = 2011 | pmid = 21374721 | pmc =3076786 }}
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1 : Proteins
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