2ns7

How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor

spinqualitylabelsall models 2ns7, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ns7 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2tct, 1qpi, 2ns8 Gene: tetR (Escherichia coli) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tetracycline repressor protein

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