The Proline/Glycine-Rich Region of the Biofilm Adhesion Protein Aap Forms an Extended Stalk that Resists Compaction

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• 作者：Alexander E. Yarawsky¹ ; ² ; Lance R. English³ ; Steven T. Whitten³ ; Andrew B. Herr² ; ⁴ ; ^{andrew.herr@cchmc.org} ; ^{andrew.herr@uc.edu}
• 关键词：Aap ; accumulation-associated protein ; PGR ; proline/glycine-rich region ; IDP ; intrinsically disordered protein ; PPII ; polyproline type II ; TMAO ; trimethylamine N-oxide ; TFE ; 2 ; 2 ; 2-trifluoroethanol ; PNAG ; poly-N-acetylglucosamine ; His ; hexahistidine ; MBP ; maltose-binding protein ; TEV ; tobacco etch virus ; AUC ; analytical ultracentrifugation ; Rh ; hydrodynamic radius ; SEC ; size-exclusion chromatography ; KD ; thermodynamic retention factor ; FCR ; fraction of charged residue ; NCPR ; net charge per residue
• 刊名：Journal of Molecular Biology
• 出版年：2017
• 出版时间：20 January 2017
• 年：2017
• 卷：429
• 期：2
• 页码：261-279
• 全文大小：1716 K
• 卷排序：429

文摘

Intercellular adhesion in Staphylococcus epidermidis biofilms is mediated by Aap. Aap's C-terminal proline/glycine-rich region (PGR) is intrinsically disordered. PGR forms an elongated monomer with high polyproline type II helix content. PGR is resistant to compaction by temperature or cosolvents such as 2,2,2-trifluoroethanol and trimethylamine N-oxide. PGR functions as an elongated stalk, projecting Aap functional domains outward