Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region.

doi:10.1016/j.jmb.2006.05.010

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Article

Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region.

Journal of molecular biology - 7 Jul 2006

Minamino Tohru, Kazetani Ken-ichi, Tahara Aiko, Suzuki Hirofumi, Furukawa Yukio, Kihara May, Namba Keiichi

Abstract excerpt

Salmonella FliI is the flagellar ATPase which converts the energy of ATP hydrolysis into the export of flagellar proteins. It forms a ring-shaped oligomer in the presence of ATP, its analogs, or phospholipids. The extreme N-terminal region of FliI has an unstable conformation and is responsible for the interaction with other components of the export apparatus and for regulation of the catalytic mechanism. To...

Topics

Bacterial Proteins
Circular Dichroism
Escherichia coli
Flagella
Genetic Complementation Test
Models, Biological
Mutation
Phospholipids
Protein Structure, Quaternary
Protein Transport
Proton-Translocating ATPases
Salmonella
Substrate Specificity

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Identifiers

PMID: 16780875
DOI: 10.1016/j.jmb.2006.05.010

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