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7pt0

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7pt0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PT0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7pt0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PT0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></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=7pt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pt0 OCA], [https://pdbe.org/7pt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pt0 RCSB], [https://www.ebi.ac.uk/pdbsum/7pt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pt0 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=7pt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pt0 OCA], [https://pdbe.org/7pt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pt0 RCSB], [https://www.ebi.ac.uk/pdbsum/7pt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pt0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/Q9KYU4_STRCO Q9KYU4_STRCO]]
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[https://www.uniprot.org/uniprot/Q9KYU4_STRCO Q9KYU4_STRCO]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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TetR/AcrR-like transcription regulators enable bacteria to sense a wide variety of chemical compounds and to dynamically adapt the expression levels of specific genes in response to changing growth conditions. Here, we describe the structural characterisation of SCO3201, an atypical TetR/AcrR family member from Streptomyces coelicolor that strongly represses antibiotic production and morphological development under conditions of overexpression. We present crystal structures of SCO3201 in its ligand-free state as well as in complex with an unknown inducer, potentially a polyamine. In the ligand-free state, the DNA-binding domains of the SCO3201 dimer are held together in an unusually compact conformation and, as a result, the regulator cannot span the distance between the two half-sites of its operator. Interaction with the ligand coincides with a major structural rearrangement and partial conversion of the so-called hinge helix (alpha4) to a 310 -conformation, markedly increasing the distance between the DNA-binding domains. In sharp contrast to what was observed for other TetR/AcrR-like regulators, the increased interdomain distance might facilitate rather than abrogate interaction of the dimer with the operator. Such a 'reverse' induction mechanism could expand the regulatory repertoire of the TetR/AcrR family and may explain the dramatic impact of SCO3201 overexpression on the ability of S. coelicolor to generate antibiotics and sporulate.
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Crystal structures of free and ligand-bound forms of the TetR/AcrR-like regulator SCO3201 from Streptomyces coelicolor suggest a novel allosteric mechanism.,Werten S, Waack P, Palm GJ, Virolle MJ, Hinrichs W FEBS J. 2022 Aug 26. doi: 10.1111/febs.16606. PMID:36017630<ref>PMID:36017630</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7pt0" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

SCO3201 with putative ligand

PDB ID 7pt0

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