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Catabolite Control Protein A : ウィキペディア英語版 | Catabolite Control Protein A
Catabolite Control Protein A (CcpA) is a master regulator of carbon metabolism in gram-positive bacteria. It is a member of the LacI/GalR transcription regulator family.〔 In contrast to most LacI/GalR proteins, CcpA is allosterically regulated principally by a protein-protein interaction, rather than a protein-small molecule interaction.〔 CcpA interacts with the phosphorylated form of Hpr〔 and Crh, which is formed when high concentrations of glucose or fructose-1,6-bisphosphate〔 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.〔 Small molecules glucose-6-phosphate and fructose-1,6-bisphosphate are also known allosteric effectors, fine-tuning CcpA function. == Structure ==
The DNA-binding functional unit of CcpA consists of a homodimer.〔 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.〔 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. 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.〔 Binding to phosphorylated Hpr/Crh occurs along the regulatory domain's N-subdomain.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Catabolite Control Protein A」の詳細全文を読む
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