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| | <StructureSection load='3e3c' size='340' side='right'caption='[[3e3c]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='3e3c' size='340' side='right'caption='[[3e3c]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3e3c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E3C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3e3c]] is a 2 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=3E3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E3C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HHG:(2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL+HEXANOATE'>HHG</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ovs|2ovs]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HHG:(2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL+HEXANOATE'>HHG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECs4578 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=3e3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e3c OCA], [https://pdbe.org/3e3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e3c RCSB], [https://www.ebi.ac.uk/pdbsum/3e3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e3c ProSAT]</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=3e3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e3c OCA], [https://pdbe.org/3e3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e3c RCSB], [https://www.ebi.ac.uk/pdbsum/3e3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e3c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7DB61_ECO57 Q7DB61_ECO57] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jobichen, C]] | + | [[Category: Jobichen C]] |
| - | [[Category: Sivaraman, J]] | + | [[Category: Sivaraman J]] |
| - | [[Category: Grlr]]
| + | |
| - | [[Category: Lee regulator]]
| + | |
| - | [[Category: Lipid binding]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| Structural highlights
Function
Q7DB61_ECO57
Publication Abstract from PubMed
Lipocalins are a broad family of proteins identified initially in eukaryotes and more recently in Gram-negative bacteria. The functions of lipocalin or lipid-binding proteins are often elusive and very diverse. Recently, we have determined the structure of GrlR (global regulator of LEE repressor), which plays a key role in the regulation of LEE (locus of enterocyte effacement) proteins. GrlR adopts a lipocalin-like fold that is composed of an eight-stranded beta-barrel followed by an alpha-helix at the C-terminus. GrlR has a highly hydrophobic cavity region and could be a potential transporter of lipophilic molecules. To verify this hypothesis, we carried out structure-based analysis of GrlR, determined the structure of the lipid-GrlR complex and measured the binding of lipid to recombinant GrlR by ITC (isothermal titration calorimetry). In addition, we identified phosphatidylglycerol and phosphatidylethanolamine as the endogenously bound lipid species of GrlR using electrospray-ionization MS. Furthermore, we have shown that the lipid-binding property of GrlR is similar to that of its closest lipocalin structural homologue, beta-lactoglobulin. Our studies demonstrate the hitherto unknown lipid-binding property of GrlR.
Identification and characterization of the lipid-binding property of GrlR, a locus of enterocyte effacement regulator.,Jobichen C, Fernandis AZ, Velazquez-Campoy A, Leung KY, Mok YK, Wenk MR, Sivaraman J Biochem J. 2009 May 13;420(2):191-9. PMID:19228114[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jobichen C, Fernandis AZ, Velazquez-Campoy A, Leung KY, Mok YK, Wenk MR, Sivaraman J. Identification and characterization of the lipid-binding property of GrlR, a locus of enterocyte effacement regulator. Biochem J. 2009 May 13;420(2):191-9. PMID:19228114 doi:10.1042/BJ20081588
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