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| | <StructureSection load='4tv7' size='340' side='right'caption='[[4tv7]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='4tv7' size='340' side='right'caption='[[4tv7]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tv7]] is a 4 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=4TV7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TV7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tv7]] is a 4 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=4TV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TV7 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tv7 OCA], [https://pdbe.org/4tv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tv7 RCSB], [https://www.ebi.ac.uk/pdbsum/4tv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tv7 ProSAT]</span></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=4tv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tv7 OCA], [http://pdbe.org/4tv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tv7 RCSB], [http://www.ebi.ac.uk/pdbsum/4tv7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tv7 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 4tv7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4tv7" 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: Goto, M]] | + | [[Category: Goto M]] |
| - | [[Category: Okuda, K]] | + | [[Category: Okuda K]] |
| - | [[Category: Yoshimura, T]] | + | [[Category: Yoshimura T]] |
| - | [[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
MocR/GabR family proteins are widely distributed prokaryotic transcriptional regulators containing pyridoxal 5'-phosphate (PLP), a coenzyme form of vitamin B6. The Bacillus subtilis GabR, probably the most extensively studied MocR/GabR family protein, consists of an N-terminal DNA-binding domain and a PLP-binding C-terminal domain that has a structure homologous to aminotransferases. GabR suppresses transcription of gabR and activates transcription of gabT and gabD, which encode gamma-aminobutyrate (GAlphaBetaAlpha) aminotransferase and succinate semialdehyde dehydrogenase, respectively, in the presence of PLP and GABA. In this study, we examined the mechanism underlying GabR-mediated gabTD transcription with spectroscopic, crystallographic and thermodynamic studies, focusing on the function of the aminotransferase domain. Spectroscopic studies revealed that GABA forms an external aldimine with the PLP in the aminotransferase domain. Isothermal calorimetry demonstrated that two GabR molecules bind to the 51-bp DNA fragment that contains the GabR-binding region. GABA minimally affected DeltaG(binding) upon binding of GabR to the DNA fragment but greatly affected the contributions of DeltaH and DeltaS to DeltaG(binding). GABA forms an external aldimine with PLP and causes a conformational change in the aminotransferase domain, and this change likely rearranges GabR binding to the promoter and thus activates gabTD transcription.
Role of the aminotransferase domain in Bacillus subtilis GabR, a pyridoxal 5'-phosphate-dependent transcriptional regulator.,Okuda K, Kato S, Ito T, Shiraki S, Kawase Y, Goto M, Kawashima S, Hemmi H, Fukada H, Yoshimura T Mol Microbiol. 2015 Jan;95(2):245-57. doi: 10.1111/mmi.12861. Epub 2014 Dec 8. PMID:25388514[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
- ↑ Okuda K, Kato S, Ito T, Shiraki S, Kawase Y, Goto M, Kawashima S, Hemmi H, Fukada H, Yoshimura T. Role of the aminotransferase domain in Bacillus subtilis GabR, a pyridoxal 5'-phosphate-dependent transcriptional regulator. Mol Microbiol. 2015 Jan;95(2):245-57. doi: 10.1111/mmi.12861. Epub 2014 Dec 8. PMID:25388514 doi:http://dx.doi.org/10.1111/mmi.12861
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