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| | <StructureSection load='3usy' size='340' side='right'caption='[[3usy]], [[Resolution|resolution]] 2.71Å' scene=''> | | <StructureSection load='3usy' size='340' side='right'caption='[[3usy]], [[Resolution|resolution]] 2.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3usy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3pl4 3pl4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3USY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3USY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3usy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3pl4 3pl4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3USY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3USY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3usw|3usw]]</div></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]] 2.706Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0352 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</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=3usy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3usy OCA], [https://pdbe.org/3usy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3usy RCSB], [https://www.ebi.ac.uk/pdbsum/3usy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3usy 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=3usy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3usy OCA], [https://pdbe.org/3usy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3usy RCSB], [https://www.ebi.ac.uk/pdbsum/3usy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3usy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FLIG_HELPY FLIG_HELPY]] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY.<ref>PMID:10960117</ref> <ref>PMID:22325779</ref>
| + | [https://www.uniprot.org/uniprot/FLIG_HELPY FLIG_HELPY] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY.<ref>PMID:10960117</ref> <ref>PMID:22325779</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43504]] | + | [[Category: Helicobacter pylori]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Au, S W.N]] | + | [[Category: Au SWN]] |
| - | [[Category: Lam, K H]] | + | [[Category: Lam KH]] |
| - | [[Category: Flagellar motor]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Motor switch protein]]
| + | |
| Structural highlights
Function
FLIG_HELPY One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY.[1] [2]
Publication Abstract from PubMed
Bacterial flagellar switching between counterclockwise and clockwise directions is mediated by the coupling of the chemotactic system and the motor switch complex. The conformational changes of FliG are closely associated with this switching mechanism. We present two crystal structures of FliG(MC) from Helicobacter pylori, each showing distinct domain orientations from previously solved structures. A 180 degrees rotation of the charged ridge-containing C-terminal subdomain FliG(Calpha1-6) that is prompted by the rotational freedom of Met245 psi and Phe246 phi at the MFXF motif was revealed. Studies on the swarming and swimming behavior of Escherichia coli mutants further identified the importance of the (2)(4)(5)MFXF(2)(4)(8) motif and a highly conserved residue, Asn216, in motor switching. Additionally, multiple conformations of FliG(Calpha1-6) were demonstrated by intramolecular cysteine crosslinking. The conformational flexibility of FliGc leads us to propose a model that accounts for the symmetrical torque generation process and for the dynamics of the motor.
Multiple conformations of the FliG C-terminal domain provide insight into flagellar motor switching.,Lam KH, Ip WS, Lam YW, Chan SO, Ling TK, Au SW Structure. 2012 Feb 8;20(2):315-25. PMID:22325779[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Allan E, Dorrell N, Foynes S, Anyim M, Wren BW. Mutational analysis of genes encoding the early flagellar components of Helicobacter pylori: evidence for transcriptional regulation of flagellin A biosynthesis. J Bacteriol. 2000 Sep;182(18):5274-7. PMID:10960117
- ↑ Lam KH, Ip WS, Lam YW, Chan SO, Ling TK, Au SW. Multiple conformations of the FliG C-terminal domain provide insight into flagellar motor switching. Structure. 2012 Feb 8;20(2):315-25. PMID:22325779 doi:10.1016/j.str.2011.11.020
- ↑ Lam KH, Ip WS, Lam YW, Chan SO, Ling TK, Au SW. Multiple conformations of the FliG C-terminal domain provide insight into flagellar motor switching. Structure. 2012 Feb 8;20(2):315-25. PMID:22325779 doi:10.1016/j.str.2011.11.020
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