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| | <StructureSection load='3wxx' size='340' side='right'caption='[[3wxx]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3wxx' size='340' side='right'caption='[[3wxx]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wxx]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/"aeromonas_liquefaciens"_kluyver_and_van_niel_1936 "aeromonas liquefaciens" kluyver and van niel 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WXX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wxx]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_hydrophila Aeromonas hydrophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WXX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.7Å</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acrH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=644 "Aeromonas liquefaciens" Kluyver and van Niel 1936]), aopB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=644 "Aeromonas liquefaciens" Kluyver and van Niel 1936])</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=3wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wxx OCA], [https://pdbe.org/3wxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wxx RCSB], [https://www.ebi.ac.uk/pdbsum/3wxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wxx 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=3wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wxx OCA], [https://pdbe.org/3wxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wxx RCSB], [https://www.ebi.ac.uk/pdbsum/3wxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wxx ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aeromonas liquefaciens kluyver and van niel 1936]] | + | [[Category: Aeromonas hydrophila]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Henry, Y K.M]] | + | [[Category: Henry YKM]] |
| - | [[Category: Jobichen, C]] | + | [[Category: Jobichen C]] |
| - | [[Category: Nguyen, V S]] | + | [[Category: Nguyen VS]] |
| - | [[Category: Sivaraman, J]] | + | [[Category: Sivaraman J]] |
| - | [[Category: Membrane protein-chaperone complex]]
| + | |
| - | [[Category: Translocator]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Type III secretion systems (T3SSs) are adopted by pathogenic bacteria for the transport of effector proteins into host cells through the translocon pore composed of major and minor translocator proteins. Both translocators require a dedicated chaperone for solubility. Despite tremendous efforts in the past, structural information regarding the chaperone-translocator complex and the topology of the translocon pore have remained elusive. Here, we report the crystal structure of the major translocator, AopB, from Aeromonas hydrophila AH-1 in complex with its chaperone, AcrH. Overall, the structure revealed unique interactions between the various interfaces of AopB and AcrH, with the N-terminal "molecular anchor" of AopB crossing into the "N-terminal arm" of AcrH. AopB adopts a novel fold, and its transmembrane regions form two pairs of helical hairpins. From these structural studies and associated cellular assays, we deduced the topology of the assembled T3SS translocon; both termini remain extracellular after membrane insertion.
Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly.,Nguyen VS, Jobichen C, Tan KW, Tan YW, Chan SL, Ramesh K, Yuan Y, Hong Y, Seetharaman J, Leung KY, Sivaraman J, Mok YK Structure. 2015 Nov 3;23(11):2022-31. doi: 10.1016/j.str.2015.08.014. Epub 2015, Oct 1. PMID:26439768[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nguyen VS, Jobichen C, Tan KW, Tan YW, Chan SL, Ramesh K, Yuan Y, Hong Y, Seetharaman J, Leung KY, Sivaraman J, Mok YK. Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly. Structure. 2015 Nov 3;23(11):2022-31. doi: 10.1016/j.str.2015.08.014. Epub 2015, Oct 1. PMID:26439768 doi:http://dx.doi.org/10.1016/j.str.2015.08.014
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