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• W2068659764 abstract "Crystal structure determination of catabolite control protein A (CcpA) at 2.6 Å resolution reveals for the first time the structure of a full-length apo-form LacI-GalR family repressor protein. In the crystal structures of these transcription regulators, the three-helix bundle of the DNA-binding domain has only been observed in cognate DNA complexes; it has not been observed in other crystal structures owing to its mobility. In the crystal packing of apo-CcpA, the protein–protein contacts between the N-terminal three-helix bundle and the core domain consisted of interactions between the homodimers that were similar to those between the corepressor protein HPr and the CcpA N-subdomain in the ternary DNA complex. In contrast to the DNA complex, the apo-CcpA structure reveals large subdomain movements in the core, resulting in a complete loss of contacts between the N-subdomains of the homodimer." @default.
• W2068659764 created "2016-06-24" @default.
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• W2068659764 date "2007-03-12" @default.
• W2068659764 modified "2023-09-27" @default.
• W2068659764 title "Structure of the apo form of the catabolite control protein A (CcpA) from<i>Bacillus megaterium</i>with a DNA-binding domain" @default.
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• W2068659764 doi "https://doi.org/10.1107/s1744309107008949" @default.
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