2bx9
From Proteopedia
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==Overview== | ==Overview== | ||
- | 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 .. | + | 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. |
==About this Structure== | ==About this Structure== | ||
- | 2BX9 is a | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: trp rna-binding attenuation protein]] | [[Category: trp rna-binding attenuation protein]] | ||
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:35:24 2007'' |
Revision as of 12:30, 5 November 2007
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CRYSTAL STRUCTURE OF B.SUBTILIS ANTI-TRAP PROTEIN, AN ANTAGONIST OF TRAP-RNA INTERACTIONS
Overview
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.
About this Structure
2BX9 is a Single protein structure of sequence from Bacillus subtilis with ZN as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction., Shevtsov MB, Chen Y, Gollnick P, Antson AA, Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17600-5. Epub 2005 Nov 23. PMID:16306262
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