2bx9: Difference between revisions
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==Overview== | ==Overview== | ||
In Bacillus subtilis the anti-TRAP protein (AT) is produced in response to | 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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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Antson, A | [[Category: Antson, A A.]] | ||
[[Category: Chen, Y.]] | [[Category: Chen, Y.]] | ||
[[Category: Gollnick, P.]] | [[Category: Gollnick, P.]] | ||
[[Category: Shevtsov, M | [[Category: Shevtsov, M B.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: anti-trap]] | [[Category: anti-trap]] | ||
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[[Category: trp rna-binding attenuation protein]] | [[Category: trp rna-binding attenuation protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:35 2008'' | ||
Revision as of 17:42, 21 February 2008
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CRYSTAL STRUCTURE OF B.SUBTILIS ANTI-TRAP PROTEIN, AN ANTAGONIST OF TRAP-RNA INTERACTIONS
OverviewOverview
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 StructureAbout this Structure
2BX9 is a Single protein structure of sequence from Bacillus subtilis with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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