1ucu
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ucu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ucu OCA], [http://www.ebi.ac.uk/pdbsum/1ucu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ucu RCSB]</span> | ||
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[[Category: helical reconstruction]] | [[Category: helical reconstruction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:08:46 2008'' |
Revision as of 21:08, 30 March 2008
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| , resolution 4.0Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
R-type straight flagellar filament made of full-length flagellin
Overview
The bacterial flagellar filament is a helical propeller for bacterial locomotion. It is a helical assembly of a single protein, flagellin, and its tubular structure is formed by 11 protofilaments in two distinct conformations, L- and R-type, for supercoiling. The X-ray crystal structure of a flagellin fragment lacking about 100 terminal residues revealed the protofilament structure, but the full filament structure is still essential for understanding the mechanism of supercoiling and polymerization. Here we report a complete atomic model of the R-type filament by electron cryomicroscopy. A density map obtained from image data up to 4 A resolution shows the feature of alpha-helical backbone and some large side chains. The atomic model built on the map reveals intricate molecular packing and an alpha-helical coiled coil formed by the terminal chains in the inner core of the filament, with its intersubunit hydrophobic interactions having an important role in stabilizing the filament.
About this Structure
1UCU is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy., Yonekura K, Maki-Yonekura S, Namba K, Nature. 2003 Aug 7;424(6949):643-50. PMID:12904785
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