2ns7
From Proteopedia
(New page: 200px<br /><applet load="2ns7" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ns7, resolution 2.400Å" /> '''How an in vitro sel...) |
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==Overview== | ==Overview== | ||
| - | A 16-residue peptide, called Tip, induces the tetracycline repressor TetR | + | A 16-residue peptide, called Tip, induces the tetracycline repressor TetR as efficiently as the antibiotic tetracycline when fused to the N or C terminus of another protein. This is unusual because the majority of in vitro selected peptides, such as Tip, inhibit protein function, and agonist peptides are only rarely identified. We elucidated the atomic mechanism of TetR induction by Tip from crystal structures of TetR in complex with Tip and of free TetR. Peptide induction ultimately results in the same movements of DNA reading heads, but Tip accomplishes this by very different molecular interactions from tetracycline involving important contacts to the TetR surface. As a direct consequence, an alternate pathway of allostery becomes possible that makes ample use of intersubunit interactions. For the first time it is possible to show in atomic detail how a small molecule controlled bacterial transcription factor such as TetR becomes responsive to protein-protein interactions, characteristic of gene transcription regulation in higher organisms. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Hillen, W.]] | [[Category: Hillen, W.]] | ||
[[Category: Klotzsche, M.]] | [[Category: Klotzsche, M.]] | ||
| - | [[Category: Luckner, S | + | [[Category: Luckner, S R.]] |
| - | [[Category: Muller, Y | + | [[Category: Muller, Y A.]] |
[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
[[Category: transcription regulator]] | [[Category: transcription regulator]] | ||
| - | ''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 18:10:20 2008'' |
Revision as of 16:10, 21 February 2008
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How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor
Overview
A 16-residue peptide, called Tip, induces the tetracycline repressor TetR as efficiently as the antibiotic tetracycline when fused to the N or C terminus of another protein. This is unusual because the majority of in vitro selected peptides, such as Tip, inhibit protein function, and agonist peptides are only rarely identified. We elucidated the atomic mechanism of TetR induction by Tip from crystal structures of TetR in complex with Tip and of free TetR. Peptide induction ultimately results in the same movements of DNA reading heads, but Tip accomplishes this by very different molecular interactions from tetracycline involving important contacts to the TetR surface. As a direct consequence, an alternate pathway of allostery becomes possible that makes ample use of intersubunit interactions. For the first time it is possible to show in atomic detail how a small molecule controlled bacterial transcription factor such as TetR becomes responsive to protein-protein interactions, characteristic of gene transcription regulation in higher organisms.
About this Structure
2NS7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
How an agonist peptide mimics the antibiotic tetracycline to induce Tet-repressor., Luckner SR, Klotzsche M, Berens C, Hillen W, Muller YA, J Mol Biol. 2007 May 4;368(3):780-90. Epub 2007 Feb 22. PMID:17374541
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