Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals

TitleFolding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals
Publication TypeJournal Article
Year of Publication2006
AuthorsGoobes, G., Goobes R., Schueler-Furman O., Baker D., Stayton P. S., & Drobny G. P.
JournalProceedings of the National Academy of Sciences of the United States of America
Volume103
Issue44
Pagination16083-8
Date Published2006 Oct 31
ISSN0027-8424
KeywordsAdsorption, Algorithms, Bacterial Adhesion, Collaborative Publication, Computational Biology, Crystallization, Durapatite, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Folding, Protein Structure, Tertiary, Salivary Proteins and Peptides
Abstract

Statherin is an enamel pellicle protein that inhibits hydroxyapatite (HAP) nucleation and growth, lubricates the enamel surface, and is recognized by oral bacteria in periodontal diseases. We report here from solid-state NMR measurements that the protein's C-terminal region folds into an alpha-helix upon adsorption to HAP crystals. This region contains the binding sites for bacterial fimbriae that mediate bacterial cell adhesion to the surface of the tooth. The helical segment is shown through long-range distance measurements to fold back onto the intermediate region (residues Y16-P28) defining the global fold of the protein. Statherin, previously shown to be unstructured in solution, undergoes conformation selection on its substrate mineral surface. This surface-induced folding of statherin can be related to its functionality in inhibiting HAP crystal growth and can explain how oral pathogens selectively recognize HAP-bound statherin.

Alternate JournalProc. Natl. Acad. Sci. U.S.A.
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