Download MendeleyCrystal Structure of Bacillus Subtilis Anti-Trap Protein, an Antagonist of Trap/RNA Interaction.
Shevtsov, M.B., Chen, Y., Gollnick, P., Antson, A.A.(2005) Proc Natl Acad Sci U S A 102: 17600
- PubMed: 16306262
- DOI: https://doi.org/10.1073/pnas.0508728102
- Primary Citation of Related Structures:
2BX9 - PubMed Abstract:
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 angstroms 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.
Organizational Affiliation:
York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, United Kingdom.
