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| | ==Crystal structure of the L68D variant of mLolB== | | ==Crystal structure of the L68D variant of mLolB== |
| - | <StructureSection load='3wjt' size='340' side='right' caption='[[3wjt]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='3wjt' size='340' side='right'caption='[[3wjt]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wjt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecod1 Ecod1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WJT OCA]. <br> | + | <table><tr><td colspan='2'>[[3wjt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH1 Escherichia coli DH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WJT FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wjv|3wjv]], [[3wju|3wju]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lolB, ECDH1ME8569_1148 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536056 ECOD1])</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=3wjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wjt OCA], [https://pdbe.org/3wjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wjt RCSB], [https://www.ebi.ac.uk/pdbsum/3wjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wjt ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
| + | </table> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wjt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wjt RCSB], [http://www.ebi.ac.uk/pdbsum/3wjt PDBsum]</span></td></tr> | + | |
| - | <table> | + | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | Roles of the Protruding Loop of Factor B Essential for the Localization of Lipoproteins (LolB) in the Anchoring of Bacterial Triacylated Proteins to the Outer Membrane.,Hayashi Y, Tsurumizu R, Tsukahara J, Takeda K, Narita S, Mori M, Miki K, Tokuda H J Biol Chem. 2014 Apr 11;289(15):10530-9. doi: 10.1074/jbc.M113.539270. Epub 2014, Feb 25. PMID:24569999<ref>PMID:24569999</ref> | | Roles of the Protruding Loop of Factor B Essential for the Localization of Lipoproteins (LolB) in the Anchoring of Bacterial Triacylated Proteins to the Outer Membrane.,Hayashi Y, Tsurumizu R, Tsukahara J, Takeda K, Narita S, Mori M, Miki K, Tokuda H J Biol Chem. 2014 Apr 11;289(15):10530-9. doi: 10.1074/jbc.M113.539270. Epub 2014, Feb 25. PMID:24569999<ref>PMID:24569999</ref> |
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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 3wjt" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecod1]] | + | [[Category: Escherichia coli DH1]] |
| - | [[Category: Miki, K.]] | + | [[Category: Large Structures]] |
| - | [[Category: Takeda, K.]] | + | [[Category: Miki K]] |
| - | [[Category: Tokuda, H.]] | + | [[Category: Takeda K]] |
| - | [[Category: Lola/b fold]] | + | [[Category: Tokuda H]] |
| - | [[Category: Outer membrane]]
| + | |
| - | [[Category: Transport protein]]
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| Structural highlights
Publication Abstract from PubMed
The Lol system comprising five Lol proteins, LolA through LolE, sorts Escherichia coli lipoproteins to outer membranes. The LolCDE complex, an ATP binding cassette transporter in inner membranes, releases outer membrane-specific lipoproteins in an ATP-dependent manner, causing formation of the LolA-lipoprotein complex in the periplasm. LolA transports lipoproteins through the periplasm to LolB on outer membranes. LolB is itself a lipoprotein anchored to outer membranes, although the membrane anchor is functionally dispensable. LolB then localizes lipoproteins to outer membranes through largely unknown mechanisms. The crystal structure of LolB is similar to that of LolA, and it possesses a hydrophobic cavity that accommodates acyl chains of lipoproteins. To elucidate the molecular function of LolB, a periplasmic version of LolB, mLolB, was mutagenized at various conserved residues. Despite the lack of acyl chains, most defective mutants were insoluble. However, a derivative with glutamate in place of leucine 68 was soluble and unable to localize lipoproteins to outer membranes. This leucine is present in a loop protruding from mLolB into an aqueous environment, and no analogous loop is present in LolA. Thus, leucine 68 was replaced with other residues. Replacement by acidic, but not hydrophobic, residues generated for the first time mLolB derivatives that can accept but cannot localize lipoproteins to outer membranes. Moreover, deletion of the leucine with neighboring residues impaired the lipoprotein receptor activity. Based on these observations, the roles of the protruding loop of LolB in the last step of lipoprotein sorting are discussed.
Roles of the Protruding Loop of Factor B Essential for the Localization of Lipoproteins (LolB) in the Anchoring of Bacterial Triacylated Proteins to the Outer Membrane.,Hayashi Y, Tsurumizu R, Tsukahara J, Takeda K, Narita S, Mori M, Miki K, Tokuda H J Biol Chem. 2014 Apr 11;289(15):10530-9. doi: 10.1074/jbc.M113.539270. Epub 2014, Feb 25. PMID:24569999[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hayashi Y, Tsurumizu R, Tsukahara J, Takeda K, Narita S, Mori M, Miki K, Tokuda H. Roles of the Protruding Loop of Factor B Essential for the Localization of Lipoproteins (LolB) in the Anchoring of Bacterial Triacylated Proteins to the Outer Membrane. J Biol Chem. 2014 Apr 11;289(15):10530-9. doi: 10.1074/jbc.M113.539270. Epub 2014, Feb 25. PMID:24569999 doi:http://dx.doi.org/10.1074/jbc.M113.539270
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