5deq: Difference between revisions
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<StructureSection load='5deq' size='340' side='right'caption='[[5deq]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='5deq' size='340' side='right'caption='[[5deq]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5deq]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5deq]] is a 2 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=5DEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DEQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARA:ALPHA-L-ARABINOSE'>ARA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARA:ALPHA-L-ARABINOSE'>ARA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5deq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5deq OCA], [https://pdbe.org/5deq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5deq RCSB], [https://www.ebi.ac.uk/pdbsum/5deq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5deq ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</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 5deq" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5deq" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacteroides thetaiotaomicron VPI-5482]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chang | [[Category: Chang C]] | ||
[[Category: Joachimiak | [[Category: Joachimiak A]] | ||
[[Category: Rodionov D]] | |||
[[Category: Rodionov | [[Category: Tesar C]] | ||
[[Category: Tesar | |||
Revision as of 13:32, 21 June 2023
Crystal structure of transcriptional factor AraR from Bacteroides thetaiotaomicron VPI in complex with L-arabinoseCrystal structure of transcriptional factor AraR from Bacteroides thetaiotaomicron VPI in complex with L-arabinose
Structural highlights
FunctionPublication Abstract from PubMedCarbohydrate 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 AlsoReferences
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