7C7R

Biofilm associated protein - B domain

Summary for 7C7R

• Entry DOI: 10.2210/pdb7c7r/pdb
• Descriptor: Biofilm-associated surface protein, CALCIUM ION (3 entities in total)
• Functional Keywords: cell wall-anchored surface protein, biofilm formation, cell adhesion
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 99935.50

Authors

Ma, J.F.,Xu, Z.H.,Zhang, Y.K.,Cheng, X.,Fan, S.L.,Wang, J.W.,Fang, X.Y. (deposition date: 2020-05-26, release date: 2021-05-12, Last modification date: 2024-05-29)

Primary citation

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

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: 34046916
DOI: 10.15252/embj.2020107500

Experimental method

X-RAY DIFFRACTION (3.07 Å)