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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Bibliographic Details

Published in:	The Journal of biological chemistry Vol. 284; no. 6; p. 3865
Main Authors:	Nithianantham, Stanley, Xu, Minghua, Yamada, Mitsunori, Ikegami, Akihiko, Shoham, Menachem, Han, Yiping W
Format:	Journal Article
Language:	English
Published:	United States 06.02.2009
Subjects:	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
Online Access:	Get more information
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