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| <StructureSection load='5dd4' size='340' side='right'caption='[[5dd4]], [[Resolution|resolution]] 2.56Å' scene=''> | | <StructureSection load='5dd4' size='340' side='right'caption='[[5dd4]], [[Resolution|resolution]] 2.56Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5dd4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bactn Bactn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DD4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DD4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dd4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DD4 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dd4 OCA], [https://pdbe.org/5dd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dd4 RCSB], [https://www.ebi.ac.uk/pdbsum/5dd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dd4 ProSAT]</span></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ddg|5ddg]]</td></tr>
| + | |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BT_0354 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226186 BACTN])</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=5dd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dd4 OCA], [http://pdbe.org/5dd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dd4 RCSB], [http://www.ebi.ac.uk/pdbsum/5dd4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dd4 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q8AAV8_BACTN Q8AAV8_BACTN] |
| <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 5dd4" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5dd4" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bactn]] | + | [[Category: Bacteroides thetaiotaomicron VPI-5482]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Chang, C]] | + | [[Category: Chang C]] |
- | [[Category: Joachimiak, A]] | + | [[Category: Joachimiak A]] |
- | [[Category: Structural genomic]]
| + | [[Category: Rodionov D]] |
- | [[Category: Rodionov, D]] | + | [[Category: Tesar C]] |
- | [[Category: Tesar, C]] | + | |
- | [[Category: Arar]]
| + | |
- | [[Category: Bacteroides thetaiotaomicron]]
| + | |
- | [[Category: Dna binding]]
| + | |
- | [[Category: Helix-turn-helix motif]]
| + | |
- | [[Category: Mcsg]]
| + | |
- | [[Category: Nudix fold]]
| + | |
- | [[Category: Psi-biology]]
| + | |
- | [[Category: Transcription regulator]]
| + | |
- | [[Category: Transcriptional regulator]]
| + | |
| Structural highlights
Function
Q8AAV8_BACTN
Publication Abstract from PubMed
Carbohydrate metabolism plays a crucial role in the ecophysiology of human gut microbiota. Mechanisms of transcriptional regulation of sugar catabolism in commensal and prevalent human gut bacteria such as Bacteroides thetaiotaomicron remain mostly unknown. By a combination of bioinformatics and experimental approaches, we have identified an NrtR family transcription factor (BT0354 in B. thetaiotaomicron, BtAraR) as a novel regulator controlling the arabinose utilization genes. L-arabinose was confirmed to be a negative effector of BtAraR. We have solved the crystal structures of the apo and L-arabinose-bound BtAraR proteins, as well as the complex of apo-protein with a specific DNA operator. BtAraR forms a homodimer with each subunit comprised of the ligand-binding Nudix hydrolase-like domain and the DNA-binding winged-helix-turn-helix (wHTH) domain. We have identified the residues involved in binding of L-arabinose and recognition of DNA. The majority of these residues are well conserved in the AraR orthologs in Bacteroidetes. In the structure of the BtAraR-DNA complex, we found the unique interaction of arginine intercalating its guanidinum moiety into the base pair stacking of B-DNA. L-arabinose binding induces movement of wHTH domains, resulting in a conformation unsuitable for DNA binding. Our analysis facilitates reconstruction of the metabolic and regulatory networks involved in carbohydrate utilization in human gut Bacteroides.
A novel transcriptional regulator of L-arabinose utilization in human gut bacteria.,Chang C, Tesar C, Li X, Kim Y, Rodionov DA, Joachimiak A Nucleic Acids Res. 2015 Oct 4. pii: gkv1005. PMID:26438537[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chang C, Tesar C, Li X, Kim Y, Rodionov DA, Joachimiak A. A novel transcriptional regulator of L-arabinose utilization in human gut bacteria. Nucleic Acids Res. 2015 Oct 4. pii: gkv1005. PMID:26438537 doi:http://dx.doi.org/10.1093/nar/gkv1005
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