Shevtsov, M.B., Chen, Y., Gollnick, P. and Antson, A.A. (2005) Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction. Proceedings of the National Academy of Sciences of the United States of America, 102 (49). pp. 17600-17605. ISSN 1091-6490Full text not available from this repository.
In Bacillus subtilis the anti-TRAP protein (AT) is produced in response to the accumulation of uncharged tRNATrp. 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 Å 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.
|Academic Units:||The University of York > Chemistry (York)|
|Depositing User:||York RAE Import|
|Date Deposited:||19 Feb 2009 15:09|
|Last Modified:||19 Feb 2009 15:09|
|Publisher:||National Academy of Sciences|
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