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2bx9

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==Overview==
==Overview==
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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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16306262 (full description)]]
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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==
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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]].
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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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:50:51 2007''
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''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


2bx9, resolution 2.80Å

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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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