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| | <StructureSection load='1ui5' size='340' side='right'caption='[[1ui5]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1ui5' size='340' side='right'caption='[[1ui5]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ui5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UI5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ui5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UI5 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ui6|1ui6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1ui5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ui5 OCA], [http://pdbe.org/1ui5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ui5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ui5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ui5 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=1ui5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ui5 OCA], [https://pdbe.org/1ui5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ui5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ui5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ui5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O66122_STRCH O66122_STRCH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strco]]
| + | [[Category: Horinouchi S]] |
| - | [[Category: Horinouchi, S]] | + | [[Category: Natsume R]] |
| - | [[Category: Natsume, R]] | + | [[Category: Senda T]] |
| - | [[Category: Senda, T]] | + | |
| - | [[Category: Alpha-helix-bundle]]
| + | |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Helix-turn-helix]]
| + | |
| Structural highlights
Function
O66122_STRCH
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 gamma-butyrolactone-type autoregulator/receptor systems in the Gram-positive bacterial genus Streptomyces regulate morphological differentiation or antibiotic production, or both. The autoregulator receptors act as DNA-binding proteins, and on binding their cognate ligands (gamma-butyrolactones) they are released from the DNA, thus serving as repressors. The crystal structure of CprB in Streptomyces coelicolor A3(2), a homologue of the A-factor-receptor protein, ArpA, in Streptomyces griseus, was determined. The overall structure of CprB shows that the gamma-butyrolactone receptors belong to the TetR family. CprB is composed of two domains, a DNA-binding domain and a regulatory domain. The regulatory domain contains a hydrophobic cavity, which probably serves as a ligand-binding pocket. On the basis of the crystal structure of CprB and on the analogy of the characteristics of ligand-TetR binding, the binding of gamma-butyrolactones to the regulatory domain of the receptors is supposed to induce the relocation of the DNA-binding domain through conformational changes of residues located between the ligand-binding site and the DNA-binding domain, which would result in the dissociation of the receptors from their target DNA.
Crystal structure of a gamma-butyrolactone autoregulator receptor protein in Streptomyces coelicolor A3(2).,Natsume R, Ohnishi Y, Senda T, Horinouchi S J Mol Biol. 2004 Feb 13;336(2):409-19. PMID:14757054[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Natsume R, Ohnishi Y, Senda T, Horinouchi S. Crystal structure of a gamma-butyrolactone autoregulator receptor protein in Streptomyces coelicolor A3(2). J Mol Biol. 2004 Feb 13;336(2):409-19. PMID:14757054
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