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| | <StructureSection load='5uwb' size='340' side='right'caption='[[5uwb]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5uwb' size='340' side='right'caption='[[5uwb]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uwb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Psepk Psepk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UWB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UWB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uwb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_KT2440 Pseudomonas putida KT2440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UWB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</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]] 2.604Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fcz|4fcz]]</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=5uwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uwb OCA], [https://pdbe.org/5uwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uwb RCSB], [https://www.ebi.ac.uk/pdbsum/5uwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uwb ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ttg2D, PP_0961 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160488 PSEPK])</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=5uwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uwb OCA], [http://pdbe.org/5uwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uwb RCSB], [http://www.ebi.ac.uk/pdbsum/5uwb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uwb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q88P91_PSEPK Q88P91_PSEPK] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Psepk]] | + | [[Category: Pseudomonas putida KT2440]] |
| - | [[Category: Bhabha, G]] | + | [[Category: Bhabha G]] |
| - | [[Category: Ekiert, D C]] | + | [[Category: Ekiert DC]] |
| - | [[Category: Lipid-binding]]
| + | |
| - | [[Category: Mlac]]
| + | |
| - | [[Category: Periplasmic]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
Q88P91_PSEPK
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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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