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| | <StructureSection load='5x03' size='340' side='right'caption='[[5x03]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5x03' size='340' side='right'caption='[[5x03]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x03]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X03 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X03 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x03]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X03 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABU:GAMMA-AMINO-BUTANOIC+ACID'>ABU</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gabR, ycnF, BSU03890 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABU:GAMMA-AMINO-BUTANOIC+ACID'>ABU</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x03 OCA], [http://pdbe.org/5x03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x03 RCSB], [http://www.ebi.ac.uk/pdbsum/5x03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x03 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=5x03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x03 OCA], [https://pdbe.org/5x03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x03 RCSB], [https://www.ebi.ac.uk/pdbsum/5x03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x03 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GABR_BACSU GABR_BACSU]] Activates the transcription of the gabTD operon. Is also a repressor of its own expression, both in the presence and absence of GABA. Binds specifically to the DNA region overlapping the -35 region of the gabT promoter and the -10 and +1 regions of the gabR promoter. Principally regulates the utilization of gamma-aminobutyrate.<ref>PMID:12123465</ref> <ref>PMID:15223311</ref> | + | [https://www.uniprot.org/uniprot/GABR_BACSU GABR_BACSU] Activates the transcription of the gabTD operon. Is also a repressor of its own expression, both in the presence and absence of GABA. Binds specifically to the DNA region overlapping the -35 region of the gabT promoter and the -10 and +1 regions of the gabR promoter. Principally regulates the utilization of gamma-aminobutyrate.<ref>PMID:12123465</ref> <ref>PMID:15223311</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5x03" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5x03" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lee, K S]] | + | [[Category: Lee KS]] |
| - | [[Category: Park, S A]] | + | [[Category: Park SA]] |
| - | [[Category: Aminotransferase-like domain]]
| + | |
| - | [[Category: External schiff base]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcriptional regulator]]
| + | |
| Structural highlights
Function
GABR_BACSU Activates the transcription of the gabTD operon. Is also a repressor of its own expression, both in the presence and absence of GABA. Binds specifically to the DNA region overlapping the -35 region of the gabT promoter and the -10 and +1 regions of the gabR promoter. Principally regulates the utilization of gamma-aminobutyrate.[1] [2]
Publication Abstract from PubMed
Bacillus subtilis GabR (BsGabR) is involved in the gamma-aminobutyric acid (GABA) catabolism as a transcriptional regulator, consisting of an N-terminal helix-turn-helix DNA-binding domain and a C-terminal aminotransferase-like (AT-like) domain. Research on the C-terminal AT-like domain of BsGabR (BsGabR-CTD) has focused on the interaction with GABA as an effector, but most its functional details remain unclear. To understand the underlying mechanism, we report the crystal structure of BsGabR-CTD in complex with pyridoxal 5'-phosphate (PLP) and GABA at 2.0 A resolution. The structure of ligand-bound BsGabR-CTD revealed two distinct monomeric states in a homodimer. One subunit is a closed-form containing the PLP-GABA adduct, and the other subunit is a PLP-bound open-form. Our structural studies provide a detailed mechanism indicating that the open-to-closed transition by the binding of GABA induces the conformational rearrangement of BsGabR-CTD, which may trigger the activation of transcription.
Crystal structure of the C-terminal domain of Bacillus subtilis GabR reveals a closed conformation by gamma-aminobutyric acid binding, inducing transcriptional activation.,Park SA, Park YS, Lee KS Biochem Biophys Res Commun. 2017 May 27;487(2):287-291. doi:, 10.1016/j.bbrc.2017.04.052. Epub 2017 Apr 12. PMID:28412355[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Belitsky BR, Sonenshein AL. GabR, a member of a novel protein family, regulates the utilization of gamma-aminobutyrate in Bacillus subtilis. Mol Microbiol. 2002 Jul;45(2):569-83. PMID:12123465
- ↑ Belitsky BR. Bacillus subtilis GabR, a protein with DNA-binding and aminotransferase domains, is a PLP-dependent transcriptional regulator. J Mol Biol. 2004 Jul 16;340(4):655-64. PMID:15223311 doi:http://dx.doi.org/10.1016/j.jmb.2004.05.020
- ↑ Park SA, Park YS, Lee KS. Crystal structure of the C-terminal domain of Bacillus subtilis GabR reveals a closed conformation by gamma-aminobutyric acid binding, inducing transcriptional activation. Biochem Biophys Res Commun. 2017 May 27;487(2):287-291. doi:, 10.1016/j.bbrc.2017.04.052. Epub 2017 Apr 12. PMID:28412355 doi:http://dx.doi.org/10.1016/j.bbrc.2017.04.052
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