1lkv

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lkv OCA], [http://www.ebi.ac.uk/pdbsum/1lkv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lkv RCSB]</span>
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'''Crystal Structure of the Middle and C-terminal Domains of the Flagellar Rotor Protein FliG'''
'''Crystal Structure of the Middle and C-terminal Domains of the Flagellar Rotor Protein FliG'''
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[[Category: Brown, P N.]]
[[Category: Brown, P N.]]
[[Category: Hill, C P.]]
[[Category: Hill, C P.]]
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[[Category: chemotaxis]]
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[[Category: Chemotaxis]]
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[[Category: flagella]]
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[[Category: Flagella]]
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[[Category: flagellar motion]]
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[[Category: Flagellar motion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:01:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:06 2008''
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Revision as of 21:01, 2 May 2008

Template:STRUCTURE 1lkv

Crystal Structure of the Middle and C-terminal Domains of the Flagellar Rotor Protein FliG


Overview

The FliG protein is essential for assembly, rotation and clockwise/counter-clockwise (CW/CCW) switching of the bacterial flagellum. About 25 copies of FliG are present in a large rotor-mounted assembly termed the 'switch complex', which also contains the proteins FliM and FliN. Mutational studies have identified the segments of FliG most crucial for flagellar assembly, rotation and switching. The structure of the C-terminal domain, which functions specifically in rotation, was reported previously. Here, we describe the crystal structure of a larger fragment of the FliG protein from Thermotoga maritima, which encompasses the middle and C-terminal parts of the protein (termed FliG-MC). The FliG-MC molecule consists of two compact globular domains, linked by an alpha-helix and an extended segment that contains a well-conserved Gly-Gly motif. Mutational studies indicate that FliM binds to both of the globular domains, and given the flexibility of the linking segment, FliM is likely to determine the relative orientation of the domains in the flagellum. We propose a model for the organization of FliG-MC molecules in the flagellum, and suggest that CW/CCW switching might occur by movement of the C-terminal domain relative to other parts of FliG, under the control of FliM.

About this Structure

1LKV is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG., Brown PN, Hill CP, Blair DF, EMBO J. 2002 Jul 1;21(13):3225-34. PMID:12093724 Page seeded by OCA on Sat May 3 00:01:15 2008

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