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| | <StructureSection load='5uwa' size='340' side='right'caption='[[5uwa]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='5uwa' size='340' side='right'caption='[[5uwa]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uwa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UWA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uwa]] 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=5UWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UWA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8ND:(2S)-3-(2-AMINOETHOXY)PROPANE-1,2-DIYL+DIHEXADECANOATE'>8ND</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]] 1.501Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uvn|5uvn]], [[5uw2|5uw2]], [[5uw8|5uw8]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8ND:(2S)-3-(2-AMINOETHOXY)PROPANE-1,2-DIYL+DIHEXADECANOATE'>8ND</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mlaC, yrbC, b3192, JW3159 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5uwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uwa OCA], [https://pdbe.org/5uwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uwa RCSB], [https://www.ebi.ac.uk/pdbsum/5uwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uwa ProSAT]</span></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=5uwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uwa OCA], [http://pdbe.org/5uwa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uwa RCSB], [http://www.ebi.ac.uk/pdbsum/5uwa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uwa ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MLAC_ECOLI MLAC_ECOLI]] Actively prevents phospholipid accumulation at the cell surface. Probably maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. May transfer phospholipid across the periplasmic space and deliver it to the MlaFEDB complex at the inner membrane.<ref>PMID:19383799</ref> | + | [https://www.uniprot.org/uniprot/MLAC_ECOLI MLAC_ECOLI] Actively prevents phospholipid accumulation at the cell surface. Probably maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. May transfer phospholipid across the periplasmic space and deliver it to the MlaFEDB complex at the inner membrane.<ref>PMID:19383799</ref> |
| | <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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhabha, G]] | + | [[Category: Bhabha G]] |
| - | [[Category: Ekiert, D C]] | + | [[Category: Ekiert DC]] |
| - | [[Category: Bacterial lipid transport]]
| + | |
| - | [[Category: Phospholipid-binding protein]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
MLAC_ECOLI Actively prevents phospholipid accumulation at the cell surface. Probably maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. May transfer phospholipid across the periplasmic space and deliver it to the MlaFEDB complex at the inner membrane.[1]
Publication Abstract from PubMed
How phospholipids are trafficked between the bacterial inner and outer membranes through the hydrophilic space of the periplasm is not known. We report that members of the mammalian cell entry (MCE) protein family form hexameric assemblies with a central channel capable of mediating lipid transport. The E. coli MCE protein, MlaD, forms a ring associated with an ABC transporter complex in the inner membrane. A soluble lipid-binding protein, MlaC, ferries lipids between MlaD and an outer membrane protein complex. In contrast, EM structures of two other E. coli MCE proteins show that YebT forms an elongated tube consisting of seven stacked MCE rings, and PqiB adopts a syringe-like architecture. Both YebT and PqiB create channels of sufficient length to span the periplasmic space. This work reveals diverse architectures of highly conserved protein-based channels implicated in the transport of lipids between the membranes of bacteria and some eukaryotic organelles.
Architectures of Lipid Transport Systems for the Bacterial Outer Membrane.,Ekiert DC, Bhabha G, Isom GL, Greenan G, Ovchinnikov S, Henderson IR, Cox JS, Vale RD Cell. 2017 Apr 6;169(2):273-285.e17. doi: 10.1016/j.cell.2017.03.019. PMID:28388411[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Malinverni JC, Silhavy TJ. An ABC transport system that maintains lipid asymmetry in the gram-negative outer membrane. Proc Natl Acad Sci U S A. 2009 May 12;106(19):8009-14. doi:, 10.1073/pnas.0903229106. Epub 2009 Apr 21. PMID:19383799 doi:http://dx.doi.org/10.1073/pnas.0903229106
- ↑ Ekiert DC, Bhabha G, Isom GL, Greenan G, Ovchinnikov S, Henderson IR, Cox JS, Vale RD. Architectures of Lipid Transport Systems for the Bacterial Outer Membrane. Cell. 2017 Apr 6;169(2):273-285.e17. doi: 10.1016/j.cell.2017.03.019. PMID:28388411 doi:http://dx.doi.org/10.1016/j.cell.2017.03.019
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