![]() ![]() ![]() ![]() AmtR has several unique structural features that appear to be invariant among AmtR proteins, which may be related to its regulation by the nitrogen-sensing trimeric protein GlnK rather than by small-molecule effectors. These structures reveal an all-α homodimeric TetR family regulator composed of a helix–turn–helix-hosting N-terminal DNA-binding domain and a C-terminal dimerization domain. glutamicum, in apo (2.25-Å and 2.65-Å resolution) and DNA-bound (3-Å resolution) forms. Here, we report crystal structures of AmtR, the global nitrogen regulator of C. Corynebacterium glutamicum is a bacterium used for industrial amino acid production, and understanding its metabolic pathway regulation is of high biotechnological interest. ![]()
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