7C7U
Biofilm associated protein - BSP domain
7C7U の概要
エントリーDOI | 10.2210/pdb7c7u/pdb |
分子名称 | Biofilm-associated surface protein, CALCIUM ION (3 entities in total) |
機能のキーワード | cell wall-anchored surface protein, biofilm formation, cell adhesion |
由来する生物種 | Staphylococcus aureus |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 131585.01 |
構造登録者 | Ma, J.F.,Xu, Z.H.,Zhang, Y.K.,Cheng, X.,Fan, S.L.,Wang, J.W.,Fang, X.Y. (登録日: 2020-05-26, 公開日: 2021-05-12, 最終更新日: 2023-11-29) |
主引用文献 | Ma, J.,Cheng, X.,Xu, Z.,Zhang, Y.,Valle, J.,Fan, S.,Zuo, X.,Lasa, I.,Fang, X. Structural mechanism for modulation of functional amyloid and biofilm formation by Staphylococcal Bap protein switch. Embo J., 40:e107500-e107500, 2021 Cited by PubMed Abstract: The Staphylococcal Bap proteins sense environmental signals (such as pH, [Ca ]) to build amyloid scaffold biofilm matrices via unknown mechanisms. We here report the crystal structure of the aggregation-prone region of Staphylococcus aureus Bap which adopts a dumbbell-shaped fold. The middle module (MM) connecting the N-terminal and C-terminal lobes consists of a tandem of novel double-Ca -binding motifs involved in cooperative interaction networks, which undergoes Ca -dependent order-disorder conformational switches. The N-terminal lobe is sufficient to mediate amyloid aggregation through liquid-liquid phase separation and maturation, and subsequent biofilm formation under acidic conditions. Such processes are promoted by disordered MM at low [Ca ] but inhibited by ordered MM stabilized by Ca binding, with inhibition efficiency depending on structural integrity of the interaction networks. These studies illustrate a novel protein switch in pathogenic bacteria and provide insights into the mechanistic understanding of Bap proteins in modulation of functional amyloid and biofilm formation, which could be implemented in the anti-biofilm drug design. PubMed: 34046916DOI: 10.15252/embj.2020107500 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.93 Å) |
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