2bx9: Difference between revisions

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.

2BX9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BX9 OCA].  

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 14:35:24 2007''