2BX9

Crystal structure of B.subtilis Anti-TRAP protein, an antagonist of TRAP-RNA interactions

Summary for 2BX9

• Entry DOI: 10.2210/pdb2bx9/pdb
• Descriptor: TRYPTOPHAN RNA-BINDING ATTENUATOR PROTEIN-INHIBITORY PROTEIN, ZINC ION (3 entities in total)
• Functional Keywords: transcription regulation, anti-trap
• Biological source: BACILLUS SUBTILIS
• Cellular location: Cytoplasm (Probable): O31466
• Total number of polymer chains: 12
• Total formula weight: 68651.69

Authors

Shevtsov, M.B.,Chen, Y.,Gollnick, P.,Antson, A.A. (deposition date: 2005-07-26, release date: 2005-11-30, Last modification date: 2024-10-23)

Primary citation

Shevtsov, M.B.,Chen, Y.,Gollnick, P.,Antson, A.A.
Crystal Structure of Bacillus Subtilis Anti-Trap Protein, an Antagonist of Trap/RNA Interaction.
Proc.Natl.Acad.Sci.USA, 102:17600-, 2005

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.

PubMed: 16306262
DOI: 10.1073/PNAS.0508728102

Experimental method

X-RAY DIFFRACTION (2.8 Å)