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| <StructureSection load='6oih' size='340' side='right'caption='[[6oih]], [[Resolution|resolution]] 3.85Å' scene=''> | | <StructureSection load='6oih' size='340' side='right'caption='[[6oih]], [[Resolution|resolution]] 3.85Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6oih]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6an7 6an7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OIH FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6oih]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6an7 6an7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OIH FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</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]] 3.85Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6m96|6m96]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">abcT4, aq_1094 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE]), abcT3, aq_1095 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</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=6oih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oih OCA], [https://pdbe.org/6oih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oih RCSB], [https://www.ebi.ac.uk/pdbsum/6oih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oih 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=6oih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oih OCA], [http://pdbe.org/6oih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oih RCSB], [http://www.ebi.ac.uk/pdbsum/6oih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oih ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/O67181_AQUAE O67181_AQUAE] |
| O-antigens are cell surface polysaccharides of many Gram-negative pathogens that aid in escaping innate immune responses. A widespread O-antigen biosynthesis mechanism involves the synthesis of the lipid-anchored polymer on the cytosolic face of the inner membrane, followed by transport to the periplasmic side where it is ligated to the lipid A core to complete a lipopolysaccharide molecule. In this pathway, transport to the periplasm is mediated by an ATP-binding cassette (ABC) transporter, called Wzm-Wzt. Here we present the crystal structure of the Wzm-Wzt homologue from Aquifex aeolicus in an open conformation. The transporter forms a transmembrane channel that is sufficiently wide to accommodate a linear polysaccharide. Its nucleotide-binding domain and a periplasmic extension form 'gate helices' at the cytosolic and periplasmic membrane interfaces that probably serve as substrate entry and exit points. Site-directed mutagenesis of the gates impairs in vivo O-antigen secretion in the Escherichia coli prototype. Combined with a closed structure of the isolated nucleotide-binding domains, our structural and functional analyses suggest a processive O-antigen translocation mechanism, which stands in contrast to the classical alternating access mechanism of ABC transporters.
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| Architecture of a channel-forming O-antigen polysaccharide ABC transporter.,Bi Y, Mann E, Whitfield C, Zimmer J Nature. 2018 Jan 18;553(7688):361-365. doi: 10.1038/nature25190. Epub 2018 Jan, 10. PMID:29320481<ref>PMID:29320481</ref>
| | ==See Also== |
| | | *[[ABC transporter 3D structures|ABC transporter 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6oih" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Aquae]] | | [[Category: Aquifex aeolicus VF5]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Bi, Y]] | | [[Category: Bi Y]] |
| [[Category: Zimmer, J]] | | [[Category: Zimmer J]] |
| [[Category: O-antigen polysaccharide abc transporter]]
| |
| [[Category: Transport protein]]
| |