5t77: Difference between revisions

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 <StructureSection load='5t77' size='340' side='right'caption='[[5t77]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5t77]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Theab Theab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T77 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5T77 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5t77]] 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=5T77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T77 FirstGlance]. <br>
-</td></tr><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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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>, <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]] 2&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mviN, THA_1814 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=484019 THEAB])</td></tr>
+<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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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>, <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'>[http://proteopedia.org/fgij/fg.htm?mol=5t77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t77 OCA], [http://pdbe.org/5t77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t77 RCSB], [http://www.ebi.ac.uk/pdbsum/5t77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t77 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=5t77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t77 OCA], [https://pdbe.org/5t77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t77 RCSB], [https://www.ebi.ac.uk/pdbsum/5t77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t77 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/B7IE18_THEAB B7IE18_THEAB]] Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.[PIRNR:PIRNR002869]
+[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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Peptidoglycan (PG) protects bacteria from osmotic lysis, and its biogenesis is a key antibiotic target. A central step in PG biosynthesis is flipping of the lipid-linked PG precursor lipid II across the cytoplasmic membrane for subsequent incorporation into PG. MurJ, part of the multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) transporter superfamily, was recently shown to carry out this process. However, understanding of how MurJ flips lipid II, and of how MOP transporters operate in general, remains limited due to a lack of structural information. Here we present a crystal structure of MurJ from Thermosipho africanus in an inward-facing conformation at 2.0-A resolution. A hydrophobic groove is formed by two C-terminal transmembrane helices, which leads into a large central cavity that is mostly cationic. Our studies not only provide the first structural glimpse of MurJ but also suggest that alternating access is important for MurJ function, which may be applicable to other MOP superfamily transporters.
-Crystal structure of the MOP flippase MurJ in an inward-facing conformation.,Kuk AC, Mashalidis EH, Lee SY Nat Struct Mol Biol. 2016 Dec 26. doi: 10.1038/nsmb.3346. PMID:28024149<ref>PMID:28024149</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5t77" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
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 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Theab]]
+[[Category: Thermosipho africanus TCF52B]]
-[[Category: Kuk, A C.Y]]
+[[Category: Kuk ACY]]
-[[Category: Lee, S Y]]
+[[Category: Lee S-Y]]
-[[Category: Flippase]]
-[[Category: Peptidoglycan]]
-[[Category: Transport protein]]
-[[Category: Transporter]]