title: Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction.
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.
authors.affiliation: York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, United Kingdom.
authors.forename: Mikhail B
authors.initials: MB
authors.lastname: Shevtsov
authors.forename: Yanling
authors.initials: Y
authors.lastname: Chen
authors.forename: Paul
authors.initials: P
authors.lastname: Gollnick
authors.forename: Alfred A
authors.initials: AA
authors.lastname: Antson
mesh_terms: D001412:Bacillus subtilis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D012329:RNA, Bacterial / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000378:metabolism*; D014157:Transcription Factors / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000378:metabolism*; D015032:Zinc / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; C079092:MtrB protein, Bacteria; D012329:RNA, Bacterial; D016601:RNA-Binding Proteins; D014157:Transcription Factors; C435924:yczA protein, Bacillus subtilis; D015032:Zinc