6rgv

From Proteopedia

(Difference between revisions)

Revision as of 06:32, 6 May 2020

Truncated FljB phase 2 flagellin

Structural highlights

6rgv is a 1 chain structure with sequence from Salts. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1io1
Gene:	fljB, SL1344_2756 (SALTS)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[A0A0H3NEZ8_SALTS] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073]

Publication Abstract from PubMed

The long external filament of bacterial flagella is composed of several thousand copies of a single protein, flagellin. Here, we explore the role played by lysine methylation of flagellin in Salmonella, which requires the methylase FliB. We show that both flagellins of Salmonella enterica serovar Typhimurium, FliC and FljB, are methylated at surface-exposed lysine residues by FliB. A Salmonella Typhimurium mutant deficient in flagellin methylation is outcompeted for gut colonization in a gastroenteritis mouse model, and methylation of flagellin promotes bacterial invasion of epithelial cells in vitro. Lysine methylation increases the surface hydrophobicity of flagellin, and enhances flagella-dependent adhesion of Salmonella to phosphatidylcholine vesicles and epithelial cells. Therefore, posttranslational methylation of flagellin facilitates adhesion of Salmonella Typhimurium to hydrophobic host cell surfaces, and contributes to efficient gut colonization and host infection.

Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion.,Horstmann JA, Lunelli M, Cazzola H, Heidemann J, Kuhne C, Steffen P, Szefs S, Rossi C, Lokareddy RK, Wang C, Lemaire L, Hughes KT, Uetrecht C, Schluter H, Grassl GA, Stradal TEB, Rossez Y, Kolbe M, Erhardt M Nat Commun. 2020 Apr 24;11(1):2013. doi: 10.1038/s41467-020-15738-3. PMID:32332720^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Horstmann JA, Lunelli M, Cazzola H, Heidemann J, Kuhne C, Steffen P, Szefs S, Rossi C, Lokareddy RK, Wang C, Lemaire L, Hughes KT, Uetrecht C, Schluter H, Grassl GA, Stradal TEB, Rossez Y, Kolbe M, Erhardt M. Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion. Nat Commun. 2020 Apr 24;11(1):2013. doi: 10.1038/s41467-020-15738-3. PMID:32332720 doi:http://dx.doi.org/10.1038/s41467-020-15738-3

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6rgv"

@@ Line 3: / Line 3: @@
 <StructureSection load='6rgv' size='340' side='right'caption='[[6rgv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6rgv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salts Salts]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RGV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RGV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6rgv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salts Salts]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RGV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RGV FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1io1|1io1]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fljB, SL1344_2756 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216597 SALTS])</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=6rgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rgv OCA], [http://pdbe.org/6rgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rgv RCSB], [http://www.ebi.ac.uk/pdbsum/6rgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rgv ProSAT]</span></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=6rgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rgv OCA], [http://pdbe.org/6rgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rgv RCSB], [http://www.ebi.ac.uk/pdbsum/6rgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rgv ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 12: @@
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-Bacterial flagellar filaments are assembled by tens of thousands flagellin subunits, forming 11 helically arranged protofilaments. Each protofilament can take either of the two bistable forms L-type or R-type, having slightly different conformations and inter-protofilaments interactions. By mixing different ratios of L-type and R-type protofilaments, flagella adopt multiple filament polymorphs and promote bacterial motility. In this study, we investigated the hydrogen bonding networks at the flagellin crystal packing interface in Salmonella enterica serovar typhimurium (S. typhimurium) by site-directed mutagenesis of each hydrogen bonded residue. We identified three flagellin mutants D108A, N133A and D152A that were non-motile despite their fully assembled flagella. Mutants D108A and D152A trapped their flagellar filament into inflexible right-handed polymorphs, which resemble the previously predicted 3L/8R and 4L/7R helical forms in Calladine's model but have never been reported in vivo. Mutant N133A produces floppy flagella that transform flagellar polymorphs in a disordered manner, preventing the formation of flagellar bundles. Further, we found that the hydrogen bonding interactions around these residues are conserved and coupled to flagellin L/R transition. Therefore, we demonstrate that the hydrogen bonding networks formed around flagellin residues D108, N133 and D152 greatly contribute to flagellar bending, flexibility, polymorphisms and bacterial motility.
+The long external filament of bacterial flagella is composed of several thousand copies of a single protein, flagellin. Here, we explore the role played by lysine methylation of flagellin in Salmonella, which requires the methylase FliB. We show that both flagellins of Salmonella enterica serovar Typhimurium, FliC and FljB, are methylated at surface-exposed lysine residues by FliB. A Salmonella Typhimurium mutant deficient in flagellin methylation is outcompeted for gut colonization in a gastroenteritis mouse model, and methylation of flagellin promotes bacterial invasion of epithelial cells in vitro. Lysine methylation increases the surface hydrophobicity of flagellin, and enhances flagella-dependent adhesion of Salmonella to phosphatidylcholine vesicles and epithelial cells. Therefore, posttranslational methylation of flagellin facilitates adhesion of Salmonella Typhimurium to hydrophobic host cell surfaces, and contributes to efficient gut colonization and host infection.
-Role of flagellar hydrogen bonding in Salmonella motility and flagellar polymorphic transition.,Wang C, Lunelli M, Zschieschang E, Bosse JB, Thuenauer R, Kolbe M Mol Microbiol. 2019 Nov;112(5):1519-1530. doi: 10.1111/mmi.14377. Epub 2019 Sep, 13. PMID:31444817<ref>PMID:31444817</ref>
+Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion.,Horstmann JA, Lunelli M, Cazzola H, Heidemann J, Kuhne C, Steffen P, Szefs S, Rossi C, Lokareddy RK, Wang C, Lemaire L, Hughes KT, Uetrecht C, Schluter H, Grassl GA, Stradal TEB, Rossez Y, Kolbe M, Erhardt M Nat Commun. 2020 Apr 24;11(1):2013. doi: 10.1038/s41467-020-15738-3. PMID:32332720<ref>PMID:32332720</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

6rgv

From Proteopedia

Revision as of 06:32, 6 May 2020

Truncated FljB phase 2 flagellin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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