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| | <StructureSection load='1iwm' size='340' side='right'caption='[[1iwm]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1iwm' size='340' side='right'caption='[[1iwm]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1iwm]] is a 2 chain structure with sequence from [http://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=1IWM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IWM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1iwm]] 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=1IWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IWM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iwl|1iwl]], [[1iwn|1iwn]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwm OCA], [http://pdbe.org/1iwm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iwm RCSB], [http://www.ebi.ac.uk/pdbsum/1iwm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwm 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=1iwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwm OCA], [https://pdbe.org/1iwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iwm RCSB], [https://www.ebi.ac.uk/pdbsum/1iwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LOLB_ECOLI LOLB_ECOLI]] Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability.[HAMAP-Rule:MF_00233] | + | [https://www.uniprot.org/uniprot/LOLB_ECOLI LOLB_ECOLI] Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability.[HAMAP-Rule:MF_00233] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Matsuyama, S]] | + | [[Category: Matsuyama S]] |
| - | [[Category: Miki, K]] | + | [[Category: Miki K]] |
| - | [[Category: Miyatake, H]] | + | [[Category: Miyatake H]] |
| - | [[Category: Takeda, K]] | + | [[Category: Takeda K]] |
| - | [[Category: Tokuda, H]] | + | [[Category: Tokuda H]] |
| - | [[Category: Yokota, N]] | + | [[Category: Yokota N]] |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Unclosed beta barrel]]
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| Structural highlights
Function
LOLB_ECOLI Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability.[HAMAP-Rule:MF_00233]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Lipoproteins having a lipid-modified cysteine at the N-terminus are localized on either the inner or the outer membrane of Escherichia coli depending on the residue at position 2. Five Lol proteins involved in the sorting and membrane localization of lipoprotein are highly conserved in Gram-negative bacteria. We determined the crystal structures of a periplasmic chaperone, LolA, and an outer membrane lipoprotein receptor, LolB. Despite their dissimilar amino acid sequences, the structures of LolA and LolB are strikingly similar to each other. Both have a hydrophobic cavity consisting of an unclosed beta barrel and an alpha-helical lid. The cavity represents a possible binding site for the lipid moiety of lipoproteins. Detailed structural differences between the two proteins provide significant insights into the molecular mechanisms underlying the energy-independent transfer of lipoproteins from LolA to LolB and from LolB to the outer membrane. Furthermore, the structures of both LolA and LolB determined from different crystal forms revealed the distinct structural dynamics regarding the association and dissociation of lipoproteins. The results are discussed in the context of the current model for the lipoprotein transfer from the inner to the outer membrane through a hydrophilic environment.
Crystal structures of bacterial lipoprotein localization factors, LolA and LolB.,Takeda K, Miyatake H, Yokota N, Matsuyama S, Tokuda H, Miki K EMBO J. 2003 Jul 1;22(13):3199-209. PMID:12839983[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takeda K, Miyatake H, Yokota N, Matsuyama S, Tokuda H, Miki K. Crystal structures of bacterial lipoprotein localization factors, LolA and LolB. EMBO J. 2003 Jul 1;22(13):3199-209. PMID:12839983 doi:http://dx.doi.org/10.1093/emboj/cdg324
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