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| | ==Crystal structure of FliM-SpeE complex from H. pylori== | | ==Crystal structure of FliM-SpeE complex from H. pylori== |
| - | <StructureSection load='5x0z' size='340' side='right' caption='[[5x0z]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='5x0z' size='340' side='right'caption='[[5x0z]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x0z]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X0Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x0z]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X0Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">speE, HP_0832 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori]), HP_1031 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></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=5x0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x0z OCA], [http://pdbe.org/5x0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x0z RCSB], [http://www.ebi.ac.uk/pdbsum/5x0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x0z 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=5x0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x0z OCA], [https://pdbe.org/5x0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x0z RCSB], [https://www.ebi.ac.uk/pdbsum/5x0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x0z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SPEE_HELPY SPEE_HELPY]] Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM), which serves as an aminopropyl donor.<ref>PMID:16009566</ref> | + | [https://www.uniprot.org/uniprot/SPEE_HELPY SPEE_HELPY] Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM), which serves as an aminopropyl donor.<ref>PMID:16009566</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5x0z" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5x0z" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| - | [[Category: Au, S W.N]] | + | [[Category: Large Structures]] |
| - | [[Category: Zhang, H]] | + | [[Category: Au SWN]] |
| - | [[Category: Flagellar motor]]
| + | [[Category: Zhang H]] |
| - | [[Category: H. pylori]] | + | |
| - | [[Category: Motility]]
| + | |
| - | [[Category: Transferase-motor protein complex]]
| + | |
| Structural highlights
Function
SPEE_HELPY Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM), which serves as an aminopropyl donor.[1]
Publication Abstract from PubMed
The flagellar motor is an important virulence factor in infection by many bacterial pathogens. Motor function can be modulated by chemotactic proteins and recently-appreciated proteins that are not part of the flagellar or chemotaxis systems. How these latter proteins affect flagellar activity is not fully understood. Here, we identified spermidine synthase SpeE as an interacting partner of switch protein FliM in Helicobacter pylori using pull-down assay and mass spectrometry. To understand how SpeE contributes to flagellar motility, a speE-null mutant was generated and its motility behavior was evaluated. We found that deletion of SpeE did not affect flagellar formation, but induced clockwise rotation bias. We further determined the crystal structure of the FliM-SpeE complex at 2.7 A resolution. SpeE dimer binds to FliM with micromolar binding affinity, and their interaction is mediated through the beta1' and beta2' region of FliM middle domain. The FliM-SpeE binding interface partially overlaps with the FliM surface that interacts with FliG and is essential for proper flagellar rotational switching. By a combination of protein sequence conservation analysis and pull-down assays using FliM and SpeE orthologues in E. coli, our data suggest that FliM-SpeE association is unique to Helicobacter species. This article is protected by copyright. All rights reserved.
A putative spermidine synthase interacts with flagellar switch protein FliM and regulates motility in Helicobacter pylori.,Zhang H, Lam KH, Lam WWL, Wong SYY, Chan VSF, Au SWN Mol Microbiol. 2017 Sep 4. doi: 10.1111/mmi.13829. PMID:28868744[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee MJ, Huang CY, Sun YJ, Huang H. Cloning and characterization of spermidine synthase and its implication in polyamine biosynthesis in Helicobacter pylori strain 26695. Protein Expr Purif. 2005 Oct;43(2):140-8. PMID:16009566 doi:http://dx.doi.org/S1046-5928(05)00153-1
- ↑ Zhang H, Lam KH, Lam WWL, Wong SYY, Chan VSF, Au SWN. A putative spermidine synthase interacts with flagellar switch protein FliM and regulates motility in Helicobacter pylori. Mol Microbiol. 2017 Sep 4. doi: 10.1111/mmi.13829. PMID:28868744 doi:http://dx.doi.org/10.1111/mmi.13829
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