1a6i: Difference between revisions

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<StructureSection load='1a6i' size='340' side='right'caption='[[1a6i]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1a6i' size='340' side='right'caption='[[1a6i]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1a6i]] is a 1 chain structure with sequence from [http://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=1A6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A6I FirstGlance]. <br>
<table><tr><td colspan='2'>[[1a6i]] is a 1 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=1A6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A6I FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6i OCA], [http://pdbe.org/1a6i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a6i RCSB], [http://www.ebi.ac.uk/pdbsum/1a6i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6i ProSAT]</span></td></tr>
</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=1a6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6i OCA], [https://pdbe.org/1a6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a6i RCSB], [https://www.ebi.ac.uk/pdbsum/1a6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6i ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[[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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==See Also==
==See Also==
*[[Tetracycline repressor protein|Tetracycline repressor protein]]
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
== References ==
== References ==
<references/>
<references/>

Revision as of 12:42, 26 May 2021

TET REPRESSOR, CLASS D VARIANTTET REPRESSOR, CLASS D VARIANT

Structural highlights

1a6i is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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 X-ray crystal structure analysis of inducer-free Tet repressor, TetR, at 2.4 A resolution identifies one of two openings of the tunnel-like binding site as the entrance for the inducer tetracycline-Mg2+, [Mg Tc]+. Recognition and binding of the inducer unleashes conformational changes leading to the induced state of TetR. In the first step, the C-terminal turn of alpha-helix 6 unwinds, thereby altering the orientation of alpha-helix 4. This different orientation of alpha-helix 4 is stabilized by a series of hydrogen bonds mediated through a chain of eight water molecules. The alpha-helix 4 connects the DNA-binding domain (alpha-helices 1 to 3) to the rigid TetR core, and thus regulates gene expression through its respective orientations.

Conformational changes of the Tet repressor induced by tetracycline trapping.,Orth P, Cordes F, Schnappinger D, Hillen W, Saenger W, Hinrichs W J Mol Biol. 1998 Jun 5;279(2):439-47. PMID:9642048[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Orth P, Cordes F, Schnappinger D, Hillen W, Saenger W, Hinrichs W. Conformational changes of the Tet repressor induced by tetracycline trapping. J Mol Biol. 1998 Jun 5;279(2):439-47. PMID:9642048 doi:10.1006/jmbi.1998.1775

1a6i, resolution 2.40Å

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