3usw: Difference between revisions

Latest revision as of 12:13, 8 November 2023

Crystal structure of FliG (residues 86-343) from H. pylori

Structural highlights

3usw is a 1 chain structure with sequence from Helicobacter pylori. This structure supersedes the now removed PDB entry 3pkr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.601Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='3usw' size='340' side='right'caption='[[3usw]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3usw]] is a 1 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=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>
+<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='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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.601&#8491;</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>
+[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 ==
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 43504]]
+[[Category: Helicobacter pylori]]
 [[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]]

3usw: Difference between revisions

Latest revision as of 12:13, 8 November 2023

Crystal structure of FliG (residues 86-343) from H. pylori

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools