Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 102, Issue 49, Pages 17600-17605Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0508728102
Keywords
DnaJ; trp RNA-binding attenuation protein; tryptophan biosynthesis; protein-protein interactions
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In Bacillus subtilis the anti-TRAP protein (AT) is produced in response to the accumulation of uncharged tRNA(Trp). AT regulates expression of genes involved in tryptophan biosynthesis and transport by binding to the tryptophan-activated trp RNA-binding attenuation protein (TRAP) and preventing its interaction with several mRNAs. Here, we report the x-ray structure of AT at 2.8 angstrom resolution, showing that the protein subunits assemble into tight trimers. Four such trimers are further associated into a 12-subunit particle in which individual trimers are related by twofold and threefold symmetry axes. Twelve DnaJ-like, cysteine-rich zinc-binding domains form spikes on the surface of the dodecamer. Available data suggest several possible ways for AT to interact with the 11-subunit TRAP. Interaction between the two symmetry-mismatching molecules could be assisted by the flexible nature of AT zinc-binding domains.
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