|
|
| Line 3: |
Line 3: |
| | <StructureSection load='7amy' size='340' side='right'caption='[[7amy]], [[Resolution|resolution]] 3.75Å' scene=''> | | <StructureSection load='7amy' size='340' side='right'caption='[[7amy]], [[Resolution|resolution]] 3.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7amy]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/"oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AMY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7amy]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AMY FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flhA, C1S91_05000, C9I78_24000, CGI34_13080, D5E78_16030, E4P16_05430, F0L99_07770, WR32_16185 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=670 "Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.75Å</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=7amy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7amy OCA], [https://pdbe.org/7amy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7amy RCSB], [https://www.ebi.ac.uk/pdbsum/7amy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7amy 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=7amy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7amy OCA], [https://pdbe.org/7amy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7amy RCSB], [https://www.ebi.ac.uk/pdbsum/7amy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7amy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/A0A0F5SXE4_VIBPH A0A0F5SXE4_VIBPH]] Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.[RuleBase:RU364093]
| + | [https://www.uniprot.org/uniprot/Q87FX4_VIBPA Q87FX4_VIBPA] Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.[RuleBase:RU364093] |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Type three secretion is the mechanism of protein secretion found in bacterial flagella and injectisomes. At its centre is the export apparatus (EA), a complex of five membrane proteins through which secretion substrates pass the inner membrane. While the complex formed by four of the EA proteins has been well characterised structurally, little is known about the structure of the membrane domain of the largest subunit, FlhA in flagella, SctV in injectisomes. Furthermore, the biologically relevant nonameric assembly of FlhA/SctV has been infrequently observed and differences in conformation of the cytoplasmic portion of FlhA/SctV between open and closed states have been suggested to reflect secretion system specific differences. FlhA has been shown to bind to chaperone-substrate complexes in an open state, but in previous assembled ring structures, SctV is in a closed state. Here, we identify FlhA and SctV homologues that can be recombinantly produced in the oligomeric state and study them using cryo-electron microscopy. The structures of the cytoplasmic domains from both FlhA and SctV are in the open state and we observe a conserved interaction between a short stretch of residues at the N-terminus of the cytoplasmic domain, known as FlhAL/SctVL, with a groove on the adjacent protomer's cytoplasmic domain, which stabilises the nonameric ring assembly.
| + | |
| - | | + | |
| - | Nonameric structures of the cytoplasmic domain of FlhA and SctV in the context of the full-length protein.,Kuhlen L, Johnson S, Cao J, Deme JC, Lea SM PLoS One. 2021 Jun 18;16(6):e0252800. doi: 10.1371/journal.pone.0252800., eCollection 2021. PMID:34143799<ref>PMID:34143799</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 7amy" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Johnson, S]] | + | [[Category: Vibrio parahaemolyticus]] |
| - | [[Category: Kuhlen, L]] | + | [[Category: Johnson S]] |
| - | [[Category: Lea, S]]
| + | [[Category: Kuhlen L]] |
| - | [[Category: Export apparatus]] | + | [[Category: Lea S]] |
| - | [[Category: Motility]] | + | |
| - | [[Category: Protein export]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Secretion]]
| + | |
| - | [[Category: T3ss]]
| + | |
