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1wlg

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Revision as of 16:21, 27 October 2021

Crystal structure of FlgE31, a major fragment of the hook protein

Structural highlights

1wlg is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1io1, 1ucu
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The bacterial flagellum is a motile organelle, and the flagellar hook is a short, highly curved tubular structure that connects the flagellar motor to the long filament acting as a helical propeller. The hook is made of about 120 copies of a single protein, FlgE, and its function as a nano-sized universal joint is essential for dynamic and efficient bacterial motility and taxis. It transmits the motor torque to the helical propeller over a wide range of its orientation for swimming and tumbling. Here we report a partial atomic model of the hook obtained by X-ray crystallography of FlgE31, a major proteolytic fragment of FlgE lacking unfolded terminal regions, and by electron cryomicroscopy and three-dimensional helical image reconstruction of the hook. The model reveals the intricate molecular interactions and a plausible switching mechanism for the hook to be flexible in bending but rigid against twisting for its universal joint function.

Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism.,Samatey FA, Matsunami H, Imada K, Nagashima S, Shaikh TR, Thomas DR, Chen JZ, Derosier DJ, Kitao A, Namba K Nature. 2004 Oct 28;431(7012):1062-8. PMID:15510139^[1]

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

References

↑ Samatey FA, Matsunami H, Imada K, Nagashima S, Shaikh TR, Thomas DR, Chen JZ, Derosier DJ, Kitao A, Namba K. Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism. Nature. 2004 Oct 28;431(7012):1062-8. PMID:15510139 doi:http://dx.doi.org/10.1038/nature02997

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wlg"

@@ Line 3: / Line 3: @@
 <StructureSection load='1wlg' size='340' side='right'caption='[[1wlg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wlg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WLG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wlg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WLG FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1io1|1io1]], [[1ucu|1ucu]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1io1|1io1]], [[1ucu|1ucu]]</div></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=1wlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wlg OCA], [http://pdbe.org/1wlg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wlg RCSB], [http://www.ebi.ac.uk/pdbsum/1wlg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wlg 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=1wlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wlg OCA], [https://pdbe.org/1wlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wlg RCSB], [https://www.ebi.ac.uk/pdbsum/1wlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wlg ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 28: / Line 28: @@
 ==See Also==
-*[[Fadel A. Samatey Group|Fadel A. Samatey Group]]
-*[[Fadel A. Samatey Group (Japanese)|Fadel A. Samatey Group (Japanese)]]
 *[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
 *[[The Bacterial Flagellar Hook|The Bacterial Flagellar Hook]]
-*[[User:Fadel A. Samatey/FlgE I|User:Fadel A. Samatey/FlgE I]]
-*[[User:Fadel A. Samatey/FlgE III/Intrinsically Disordered Flagellar Rod Stretch|User:Fadel A. Samatey/FlgE III/Intrinsically Disordered Flagellar Rod Stretch]]
 == References ==
 <references/>

1wlg

From Proteopedia

Revision as of 16:21, 27 October 2021

Crystal structure of FlgE31, a major fragment of the hook protein

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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