Crystal structure of FadA adhesin from Fusobacterium nucleatum reveals a novel oligomerization motif, the leucine chain

Many bacterial appendages have filamentous structures, often composed of repeating monomers assembled in a head-to-tail manner. The mechanisms of such linkages vary. We report here a novel protein oligomerization motif identified in the FadA adhesin from the Gram-negative bacterium Fusobacterium nuc...

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Vydáno v:The Journal of biological chemistry Ročník 284; číslo 6; s. 3865
Hlavní autoři: Nithianantham, Stanley, Xu, Minghua, Yamada, Mitsunori, Ikegami, Akihiko, Shoham, Menachem, Han, Yiping W
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States 06.02.2009
Témata:
Adhesins, Bacterial - chemistry
Adhesins, Bacterial - genetics
Adhesins, Bacterial - metabolism
Amino Acid Motifs - physiology
Amino Acid Substitution
Bacterial Adhesion - physiology
Crystallography, X-Ray
Fusobacterium nucleatum - chemistry
Fusobacterium nucleatum - genetics
Fusobacterium nucleatum - metabolism
Leucine - chemistry
Leucine - genetics
Leucine - metabolism
Protein Structure, Quaternary - physiology
ISSN:0021-9258
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Shrnutí:Many bacterial appendages have filamentous structures, often composed of repeating monomers assembled in a head-to-tail manner. The mechanisms of such linkages vary. We report here a novel protein oligomerization motif identified in the FadA adhesin from the Gram-negative bacterium Fusobacterium nucleatum. The 2.0 angstroms crystal structure of the secreted form of FadA (mFadA) reveals two antiparallel alpha-helices connected by an intervening 8-residue hairpin loop. Leucine-leucine contacts play a prominent dual intra- and intermolecular role in the structure and function of FadA. First, they comprise the main association between the two helical arms of the monomer; second, they mediate the head-to-tail association of monomers to form the elongated polymers. This leucine-mediated filamentous assembly of FadA molecules constitutes a novel structural motif termed the "leucine chain." The essential role of these residues in FadA is corroborated by mutagenesis of selected leucine residues, which leads to the abrogation of oligomerization, filament formation, and binding to host cells.
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ISSN:0021-9258
DOI:10.1074/jbc.M805503200