3LD0
Crystal structure of B.licheniformis Anti-TRAP protein, an antagonist of TRAP-RNA interactions
Summary for 3LD0
| Entry DOI | 10.2210/pdb3ld0/pdb |
| Related | 2BX9 3LCZ |
| Descriptor | Inhibitor of TRAP, regulated by T-BOX (Trp) sequence RtpA, ZINC ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | anti-trap, at, trap, tryptophan rna-binding attenuation protein, transcription attenuation, antitermination, transcription factors, tryptophan biosynthesis regulation, gene regulation |
| Biological source | Bacillus licheniformis |
| Total number of polymer chains | 48 |
| Total formula weight | 279126.13 |
| Authors | Shevtsov, M.B.,Chen, Y.,Isupov, M.N.,Gollnick, P.,Antson, A.A. (deposition date: 2010-01-12, release date: 2010-02-23, Last modification date: 2023-09-06) |
| Primary citation | Shevtsov, M.B.,Chen, Y.,Isupov, M.N.,Leech, A.,Gollnick, P.,Antson, A.A. Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers. J.Struct.Biol., 170:127-133, 2010 Cited by PubMed Abstract: Anti-TRAP (AT) protein regulates expression of tryptophan biosynthetic genes by binding to the trp RNA-binding attenuation protein (TRAP) and preventing its interaction with RNA. Bacillus subtilis AT forms trimers that can either interact with TRAP or can further assemble into dodecameric particles. To determine which oligomeric forms are preserved in AT proteins of other Bacilli we studied Bacillus licheniformis AT which shares 66% sequence identity with the B. subtilis protein. We show that in solution B. licheniformis AT forms stable trimers. In crystals, depending on pH, such trimers assemble into two different types of dodecameric particles, both having 23 point group symmetry. The dodecamer formed at pH 6.0 has the same conformation as previously observed for B. subtilis AT. This dodecamer contains a large internal chamber with the volume of approximately 700 A(3), which is lined by the side chains of twelve valine residues. The presence of the hydrophobic chamber hints at the possibility that the dodecamer formation could be induced by binding of a ligand. Interestingly, in the dodecamer formed at pH 8.0 all trimers are turned inside out relatively to the form observed at pH 6.0. PubMed: 20138150DOI: 10.1016/j.jsb.2010.01.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
