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| {{STRUCTURE_2bx9| PDB=2bx9 | SCENE= }} | | {{STRUCTURE_2bx9| PDB=2bx9 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF B.SUBTILIS ANTI-TRAP PROTEIN, AN ANTAGONIST OF TRAP-RNA INTERACTIONS'''
| | ===CRYSTAL STRUCTURE OF B.SUBTILIS ANTI-TRAP PROTEIN, AN ANTAGONIST OF TRAP-RNA INTERACTIONS=== |
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| ==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 11-subunit TRAP. Interaction between the two symmetry-mismatching molecules could be assisted by the flexible nature of AT zinc-binding domains.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16306262}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16306262 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16306262}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Trap]] | | [[Category: Trap]] |
| [[Category: Trp rna-binding attenuation protein]] | | [[Category: Trp rna-binding attenuation protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:55:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:35:54 2008'' |