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| | ==Crystal Structure of full length transcription repressor LsrR from E. coli.== | | ==Crystal Structure of full length transcription repressor LsrR from E. coli.== |
| - | <StructureSection load='4go1' size='340' side='right' caption='[[4go1]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='4go1' size='340' side='right'caption='[[4go1]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4go1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GO1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4go1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GO1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1512, JW1505, lsrR, ydeW ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4go1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4go1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4go1 RCSB], [http://www.ebi.ac.uk/pdbsum/4go1 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=4go1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4go1 OCA], [https://pdbe.org/4go1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4go1 RCSB], [https://www.ebi.ac.uk/pdbsum/4go1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4go1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LSRR_ECOLI LSRR_ECOLI] Regulates transcription of many different genes. In the absence of autoinducer 2 (AI-2), represses transcription of the lsrACDBFG operon and its own transcription. In the presence of AI-2, LsrR is inactivated by binding phospho-AI-2, leading to the transcription of the lsr genes.<ref>PMID:15601708</ref> <ref>PMID:15743955</ref> <ref>PMID:17557827</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4go1" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli k-12]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Liu, X]] | + | [[Category: Large Structures]] |
| - | [[Category: Tao, Y]] | + | [[Category: Liu X]] |
| - | [[Category: Wu, M]] | + | [[Category: Tao Y]] |
| - | [[Category: Zang, J]] | + | [[Category: Wu M]] |
| - | [[Category: Hth motif]]
| + | [[Category: Zang J]] |
| - | [[Category: P-ai-2]]
| + | |
| - | [[Category: Sorc/deor family]]
| + | |
| - | [[Category: Transcription]]
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| - | [[Category: Transcription repressor]]
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| Structural highlights
Function
LSRR_ECOLI Regulates transcription of many different genes. In the absence of autoinducer 2 (AI-2), represses transcription of the lsrACDBFG operon and its own transcription. In the presence of AI-2, LsrR is inactivated by binding phospho-AI-2, leading to the transcription of the lsr genes.[1] [2] [3]
Publication Abstract from PubMed
Quorum-sensing systems are widely used by bacteria to control behavior in response to fluctuations in cell density. Several small diffusible molecules called autoinducers act as signaling molecules in quorum-sensing processes through interplay with sensors. Autoinducers modulate vital physiological functions such as nutrient acquisition, gene transcription, and virulence factor production. In Escherichia coli, LsrR serves as a global transcription regulator that responds to autoinducer-2 to regulate the expression of a variety of genes, including the lsr operon and the lsrR gene. Here, we report the crystal structure of full-length LsrR from E. coli, which has an N-terminal DNA-binding domain and a C-terminal ligand-binding domain connected by a beta-strand. Although only two molecules are found in one asymmetric unit, two neighboring dimers pack to form a tetramer that is consistent with the oligomerization state of LsrR in solution. Mutagenesis experiments and gel shift assays indicated that Gln-33 and Tyr-26 might be involved in interactions between LsrR and DNA. The LsrR-binding site for phosphorylated autoinducer-2 was predicted by structural comparisons of LsrR with CggR and SorC. Cross-linking, size exclusion chromatography, and gel shift assays determined that phosphorylated autoinducer-2 triggered the disassembly of the LsrR tetramer into dimers and reduced the DNA binding ability of LsrR. Our findings reveal a mechanism for the change in the oligomerization state of LsrR in the presence of phosphorylated autoinducer-2. Based on these observations, we propose that phosphorylated autoinducer-2 triggers the disassembly of the LsrR tetramer to activate the transcription of its target genes.
Structural Basis for Phosphorylated Autoinducer-2 Modulation of the Oligomerization State of the Global Transcription Regulator LsrR from Escherichia coli.,Wu M, Tao Y, Liu X, Zang J J Biol Chem. 2013 May 31;288(22):15878-87. doi: 10.1074/jbc.M112.417634. Epub, 2013 Apr 15. PMID:23589368[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xavier KB, Bassler BL. Regulation of uptake and processing of the quorum-sensing autoinducer AI-2 in Escherichia coli. J Bacteriol. 2005 Jan;187(1):238-48. PMID:15601708 doi:http://dx.doi.org/187/1/238
- ↑ Wang L, Hashimoto Y, Tsao CY, Valdes JJ, Bentley WE. Cyclic AMP (cAMP) and cAMP receptor protein influence both synthesis and uptake of extracellular autoinducer 2 in Escherichia coli. J Bacteriol. 2005 Mar;187(6):2066-76. PMID:15743955 doi:http://dx.doi.org/187/6/2066
- ↑ Li J, Attila C, Wang L, Wood TK, Valdes JJ, Bentley WE. Quorum sensing in Escherichia coli is signaled by AI-2/LsrR: effects on small RNA and biofilm architecture. J Bacteriol. 2007 Aug;189(16):6011-20. Epub 2007 Jun 8. PMID:17557827 doi:http://dx.doi.org/JB.00014-07
- ↑ Wu M, Tao Y, Liu X, Zang J. Structural Basis for Phosphorylated Autoinducer-2 Modulation of the Oligomerization State of the Global Transcription Regulator LsrR from Escherichia coli. J Biol Chem. 2013 May 31;288(22):15878-87. doi: 10.1074/jbc.M112.417634. Epub, 2013 Apr 15. PMID:23589368 doi:10.1074/jbc.M112.417634
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