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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals
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Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals

机译：吸附在羟基磷灰石晶体上时，折叠蛋白在C-末端的折叠

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摘要

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 a-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.
机译：Statherin是一种珐琅防护膜蛋白，可抑制羟磷灰石（HAP）的成核和生长，润滑珐琅质表面，并在牙周疾病中被口腔细菌识别。我们在这里从固态NMR测量报告，该蛋白质的C末端区域在吸附到HAP晶体后会折叠成a螺旋。该区域包含细菌菌毛的结合位点，其介导细菌细胞粘附到牙齿表面。螺旋段通过远距离测量显示为折叠回中间区域（残基Y16-P28），从而定义了蛋白质的整体折叠。以前显示在溶液中未结构化的Statherin，在其底物矿物表面上经历构象选择。这种表面诱导的伐他汀折叠可能与其抑制HAP晶体生长的功能有关，并且可以解释口腔病原体如何选择性识别HAP结合的伐他汀。

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