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| | <StructureSection load='2xgc' size='340' side='right'caption='[[2xgc]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='2xgc' size='340' side='right'caption='[[2xgc]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xgc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xgc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGC FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2x6o|2x6o]], [[1a6i|1a6i]], [[2x9d|2x9d]], [[1bjz|1bjz]], [[1qpi|1qpi]], [[2vke|2vke]], [[1du7|1du7]], [[2xgd|2xgd]], [[2trt|2trt]], [[2vkv|2vkv]], [[2xb5|2xb5]], [[1ork|1ork]], [[1bj0|1bj0]], [[2tct|2tct]], [[1bjy|1bjy]], [[2xge|2xge]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgc OCA], [https://pdbe.org/2xgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgc RCSB], [https://www.ebi.ac.uk/pdbsum/2xgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgc ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgc OCA], [https://pdbe.org/2xgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgc RCSB], [https://www.ebi.ac.uk/pdbsum/2xgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TETR2_ECOLX TETR2_ECOLX]] TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
| + | [https://www.uniprot.org/uniprot/TETR2_ECOLX TETR2_ECOLX] TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.[https://www.uniprot.org/uniprot/TETR4_ECOLX TETR4_ECOLX] TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Muller, Y A]] | + | [[Category: Muller YA]] |
| - | [[Category: Richter, J P]] | + | [[Category: Richter JP]] |
| - | [[Category: Stiebritz, M T]] | + | [[Category: Stiebritz MT]] |
| - | [[Category: Wengrzik, S]] | + | [[Category: Wengrzik S]] |
| - | [[Category: Antibiotic resistance]]
| + | |
| - | [[Category: Chimera]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulation]]
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| Structural highlights
Function
TETR2_ECOLX TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.TETR4_ECOLX TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
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
The specificity and selectivity of protein-protein interactions are of central importance for many biological processes, including signal transduction and transcription control. We used the in-house side-chain packing program MUMBO to computationally design a chain-specific heterodimeric variant of the bacterial transcription regulator tetracycline repressor (TetR), called T-A(A)B. Our goal was to engineer two different TetR chain variants, A and B, that no longer interact as AA or BB homodimers but selectively recombine to form heterodimers. Although 56 residues from each chain contribute to a dimer interface as large as 2200 A(2) in wild-type TetR, the substitution of only three residues in one chain and two residues in a second chain sufficed for generating specificity in a T-A(A)B heterodimer variant. The design was corroborated in vivo by a cell-based transcription assay, and in vitro by CD spectroscopy and X-ray crystallography. Crystal structure analyses showed that while selectivity in the B chain is achieved entirely through van der Waals repulsion, the best selectivity in the A chain is obtained for the variant with the lowest number of atoms in the interface, thus possibly leading to underpacking of the dimer interface. This results in a marked decrease in thermal stability and a drastic reduction in the solubility of the T-A(A)A(A) homodimer in comparison to the designed T-A(A)B heterodimer variant.
Computational Design of a Chain-Specific Tetracycline Repressor Heterodimer.,Stiebritz MT, Wengrzik S, Klein DL, Richter JP, Srebrzynski A, Weiler S, Muller YA J Mol Biol. 2010 Sep 10. PMID:20816982[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stiebritz MT, Wengrzik S, Klein DL, Richter JP, Srebrzynski A, Weiler S, Muller YA. Computational Design of a Chain-Specific Tetracycline Repressor Heterodimer. J Mol Biol. 2010 Sep 10. PMID:20816982 doi:10.1016/j.jmb.2010.07.055
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