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| | ==Lipoprotein-releasing system transmembrane protein LolC== | | ==Lipoprotein-releasing system transmembrane protein LolC== |
| - | <StructureSection load='5naa' size='340' side='right' caption='[[5naa]], [[Resolution|resolution]] 1.88Å' scene=''> | + | <StructureSection load='5naa' size='340' side='right'caption='[[5naa]], [[Resolution|resolution]] 1.88Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5naa]] 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=5NAA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NAA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5naa]] 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=5NAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NAA 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]] 1.88Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lolC, ycfU, b1116, JW5161 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5naa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5naa OCA], [http://pdbe.org/5naa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5naa RCSB], [http://www.ebi.ac.uk/pdbsum/5naa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5naa 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=5naa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5naa OCA], [https://pdbe.org/5naa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5naa RCSB], [https://www.ebi.ac.uk/pdbsum/5naa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5naa ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LOLC_ECOLI LOLC_ECOLI]] Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA. | + | [https://www.uniprot.org/uniprot/LOLC_ECOLI LOLC_ECOLI] Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5naa" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5naa" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ABC transporter 3D structures|ABC transporter 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Kaplan, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Periplasmic domain]] | + | [[Category: Kaplan E]] |
| - | [[Category: Protein transport]]
| + | |
| Structural highlights
Function
LOLC_ECOLI Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.
Publication Abstract from PubMed
MacB is an ABC transporter that collaborates with the MacA adaptor protein and TolC exit duct to drive efflux of antibiotics and enterotoxin STII out of the bacterial cell. Here we present the structure of ATP-bound MacB and reveal precise molecular details of its mechanism. The MacB transmembrane domain lacks a central cavity through which substrates could be passed, but instead conveys conformational changes from one side of the membrane to the other, a process we term mechanotransmission. Comparison of ATP-bound and nucleotide-free states reveals how reversible dimerization of the nucleotide binding domains drives opening and closing of the MacB periplasmic domains via concerted movements of the second transmembrane segment and major coupling helix. We propose that the assembled tripartite pump acts as a molecular bellows to propel substrates through the TolC exit duct, driven by MacB mechanotransmission. Homologs of MacB that do not form tripartite pumps, but share structural features underpinning mechanotransmission, include the LolCDE lipoprotein trafficking complex and FtsEX cell division signaling protein. The MacB architecture serves as the blueprint for understanding the structure and mechanism of an entire ABC transporter superfamily and the many diverse functions it supports.
Structure and mechanotransmission mechanism of the MacB ABC transporter superfamily.,Crow A, Greene NP, Kaplan E, Koronakis V Proc Natl Acad Sci U S A. 2017 Nov 6. pii: 201712153. doi:, 10.1073/pnas.1712153114. PMID:29109272[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Crow A, Greene NP, Kaplan E, Koronakis V. Structure and mechanotransmission mechanism of the MacB ABC transporter superfamily. Proc Natl Acad Sci U S A. 2017 Nov 6. pii: 201712153. doi:, 10.1073/pnas.1712153114. PMID:29109272 doi:http://dx.doi.org/10.1073/pnas.1712153114
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