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4fe7

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structure of xylose-binding transcription activator xylR

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Retrieved from "http://52.214.119.220/wiki/index.php/4fe7"

Categories: Escherichia coli | Large Structures | Ni L | Schumacher MA

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 ==structure of xylose-binding transcription activator xylR==
-<StructureSection load='4fe7' size='340' side='right' caption='[[4fe7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='4fe7' size='340' side='right'caption='[[4fe7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4fe7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FE7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4fe7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FE7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</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]] 2.9&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xylR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</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=4fe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fe7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fe7 RCSB], [http://www.ebi.ac.uk/pdbsum/4fe7 PDBsum]</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=4fe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fe7 OCA], [https://pdbe.org/4fe7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fe7 RCSB], [https://www.ebi.ac.uk/pdbsum/4fe7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fe7 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/XYLR_ECOLI XYLR_ECOLI] Regulatory protein for the xylBAFGHR operon.
-Escherichia coli can rapidly switch to the metabolism of l-arabinose and d-xylose in the absence of its preferred carbon source, glucose, in a process called carbon catabolite repression. Transcription of the genes required for l-arabinose and d-xylose consumption is regulated by the sugar-responsive transcription factors, AraC and XylR. E. coli represents a promising candidate for biofuel production through the metabolism of hemicellulose, which is composed of d-xylose and l-arabinose. Understanding the l-arabinose/d-xylose regulatory network is key for such biocatalyst development. Unlike AraC, which is a well-studied protein, little is known about XylR. To gain insight into XylR function, we performed biochemical and structural studies. XylR contains a C-terminal AraC-like domain. However, its N-terminal d-xylose-binding domain contains a periplasmic-binding protein (PBP) fold with structural homology to LacI/GalR transcription regulators. Like LacI/GalR proteins, the XylR PBP domain mediates dimerization. However, unlike LacI/GalR proteins, which dimerize in a parallel, side-to-side manner, XylR PBP dimers are antiparallel. Strikingly, d-xylose binding to this domain results in a helix to strand transition at the dimer interface that reorients both DNA-binding domains, allowing them to bind and loop distant operator sites. Thus, the combined data reveal the ligand-induced activation mechanism of a new family of DNA-binding proteins.
-Structures of the Escherichia coli transcription activator and regulator of diauxie, XylR: an AraC DNA-binding family member with a LacI/GalR ligand-binding domain.,Ni L, Tonthat NK, Chinnam N, Schumacher MA Nucleic Acids Res. 2012 Dec 14. PMID:23241389<ref>PMID:23241389</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Ni, L]]
+[[Category: Large Structures]]
-[[Category: Schumacher, M A]]
+[[Category: Ni L]]
-[[Category: Dna binding protein]]
+[[Category: Schumacher MA]]
-[[Category: Dna xylose]]
-[[Category: Dna-binding transcription regulator]]
-[[Category: Helix-turn-helix]]
-[[Category: Hth_arac]]
-[[Category: Pbp]]
-[[Category: Periplasmic binding protein]]

4fe7

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structure of xylose-binding transcription activator xylR

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