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| | <StructureSection load='1iwl' size='340' side='right'caption='[[1iwl]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='1iwl' size='340' side='right'caption='[[1iwl]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1iwl]] is a 1 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=1IWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IWL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1iwl]] 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=1IWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IWL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iwm|1iwm]], [[1iwn|1iwn]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1iwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwl OCA], [https://pdbe.org/1iwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iwl RCSB], [https://www.ebi.ac.uk/pdbsum/1iwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwl 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=1iwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwl OCA], [https://pdbe.org/1iwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iwl RCSB], [https://www.ebi.ac.uk/pdbsum/1iwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LOLA_ECOLI LOLA_ECOLI]] Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.<ref>PMID:11758943</ref> May act as a regulator of the RCS-phosphorelay signal transduction pathway.<ref>PMID:11758943</ref>
| + | [https://www.uniprot.org/uniprot/LOLA_ECOLI LOLA_ECOLI] Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.<ref>PMID:11758943</ref> May act as a regulator of the RCS-phosphorelay signal transduction pathway.<ref>PMID:11758943</ref> |
| | == 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: Protein transport]]
| + | |
| - | [[Category: Unclosed beta barrel]]
| + | |
| Structural highlights
Function
LOLA_ECOLI Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.[1] May act as a regulator of the RCS-phosphorelay signal transduction pathway.[2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
- ↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
- ↑ 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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