Document Detail


Crystal structure of FadA adhesin from Fusobacterium nucleatum reveals a novel oligomerization motif, the leucine chain.
MedLine Citation:
PMID:  18996848     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Stanley Nithianantham; Minghua Xu; Mitsunori Yamada; Akihiko Ikegami; Menachem Shoham; Yiping W Han
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2008-11-07
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  284     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2009 Feb 
Date Detail:
Created Date:  2009-02-02     Completed Date:  2009-04-06     Revised Date:  2013-06-04    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3865-72     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106, USA.
Data Bank Information
Bank Name/Acc. No.:
PDB/3ETW;  3ETX;  3ETY;  3ETZ
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MeSH Terms
Descriptor/Qualifier:
Adhesins, Bacterial / chemistry*,  genetics,  metabolism
Amino Acid Motifs / physiology
Amino Acid Substitution
Bacterial Adhesion / physiology
Crystallography, X-Ray
Fusobacterium nucleatum / chemistry*,  genetics,  metabolism
Leucine / chemistry,  genetics,  metabolism
Protein Structure, Quaternary / physiology
Grant Support
ID/Acronym/Agency:
K02DE16102/DE/NIDCR NIH HHS; R01DE14924/DE/NIDCR NIH HHS; R21DE17165/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Adhesins, Bacterial; 61-90-5/Leucine
Comments/Corrections

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