6nc9

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<StructureSection load='6nc9' size='340' side='right'caption='[[6nc9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='6nc9' size='340' side='right'caption='[[6nc9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6nc9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NC9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6nc9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosipho_africanus_TCF52B Thermosipho africanus TCF52B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NC9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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=6nc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nc9 OCA], [http://pdbe.org/6nc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nc9 RCSB], [http://www.ebi.ac.uk/pdbsum/6nc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nc9 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6nc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nc9 OCA], [https://pdbe.org/6nc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nc9 RCSB], [https://www.ebi.ac.uk/pdbsum/6nc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nc9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MURJ_THEAB MURJ_THEAB]] Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.[HAMAP-Rule:MF_02078]<ref>PMID:28024149</ref>
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[https://www.uniprot.org/uniprot/MURJ_THEAB MURJ_THEAB] Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.[HAMAP-Rule:MF_02078]<ref>PMID:28024149</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The biosynthesis of many polysaccharides, including bacterial peptidoglycan and eukaryotic N-linked glycans, requires transport of lipid-linked oligosaccharide (LLO) precursors across the membrane by specialized flippases. MurJ is the flippase for the lipid-linked peptidoglycan precursor Lipid II, a key player in bacterial cell wall synthesis, and a target of recently discovered antibacterials. However, the flipping mechanism of LLOs including Lipid II remains poorly understood due to a dearth of structural information. Here we report crystal structures of MurJ captured in inward-closed, inward-open, inward-occluded and outward-facing conformations. Together with mutagenesis studies, we elucidate the conformational transitions in MurJ that mediate lipid flipping, identify the key ion for function, and provide a framework for the development of inhibitors.
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Visualizing conformation transitions of the Lipid II flippase MurJ.,Kuk ACY, Hao A, Guan Z, Lee SY Nat Commun. 2019 Apr 15;10(1):1736. doi: 10.1038/s41467-019-09658-0. PMID:30988294<ref>PMID:30988294</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6nc9" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kuk, A C.Y]]
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[[Category: Thermosipho africanus TCF52B]]
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[[Category: Lee, S Y]]
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[[Category: Kuk ACY]]
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[[Category: Cell wall]]
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[[Category: Lee S-Y]]
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[[Category: Flippase]]
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[[Category: Peptidoglycan]]
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[[Category: Transport protein]]
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[[Category: Transporter]]
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Current revision

Lipid II flippase MurJ, outward-facing conformation

PDB ID 6nc9

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