Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals.
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ABSTRACT:
SUBMITTER: Goobes G
PROVIDER: S-EPMC1637540 | biostudies-literature | 2006 Oct
REPOSITORIES: biostudies-literature
Publications
Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals.
Goobes Gil G Goobes Rivka R Schueler-Furman Ora O Baker David D Stayton Patrick S PS Drobny Gary P GP
Proceedings of the National Academy of Sciences of the United States of America 20061023 44
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 l ...[more]
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