3usw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of FliG (residues 86-343) from H. pylori== | |
| + | <StructureSection load='3usw' size='340' side='right'caption='[[3usw]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3usw]] is a 1 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=3pkr 3pkr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3USW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3USW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.601Å</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=3usw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3usw OCA], [https://pdbe.org/3usw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3usw RCSB], [https://www.ebi.ac.uk/pdbsum/3usw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3usw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:22325779</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3usw" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Helicobacter pylori]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Au SWN]] | ||
| + | [[Category: Lam KH]] | ||
Current revision
Crystal structure of FliG (residues 86-343) from H. pylori
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