3QQ2

Crystal Structure of the Beta Domain of the Bordetella Autotransporter Brka

Summary for 3QQ2

• Entry DOI: 10.2210/pdb3qq2/pdb
• Descriptor: BrkA autotransporter (1 entity in total)
• Functional Keywords: beta barrel, transmembrane, membrane protein-protein transport complex, membrane protein/protein transport
• Biological source: Bordetella pertussis
• Cellular location: BrkA autotransporter: Periplasm (By similarity). Serum resistance protein BrkA: Secreted. BrkA translocator: Cell outer membrane; Multi-pass membrane protein (Probable): Q45340
• Total number of polymer chains: 3
• Total formula weight: 92965.00

Authors

Zhai, Y.,Zhang, K.,Huo, Y.,Sun, F. (deposition date: 2011-02-14, release date: 2011-04-13, Last modification date: 2023-11-01)

Primary citation

Zhai, Y.,Zhang, K.,Huo, Y.,Zhu, Y.,Zhou, Q.,Lu, J.,Black, I.,Pang, X.,Roszak, A.W.,Zhang, X.,Isaacs, N.W.,Sun, F.
Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the beta-domain pore
Biochem.J., 435:577-587, 2011

PubMed Abstract: Whooping cough (pertussis) is a highly contagious acute respiratory illness of humans caused by the Gram-negative bacterial pathogen Bordetella pertussis. The AT (autotransporter) BrkA (Bordetella serum-resistance killing protein A) is an important B. pertussis virulence factor that confers serum resistance and mediates adherence. In the present study, we have solved the crystal structure of the BrkA β-domain at 3 Å (1 Å=0.1 nm) resolution. Special features are a hairpin-like structure formed by the external loop L4, which is observed fortuitously sitting inside the pore of the crystallographic adjacent β-domain, and a previously undiscovered hydrophobic cavity formed by patches on loop L4 and β-strands S5 and S6. This adopts a ubiquitous structure characteristic of all AT β-domains. Mutagenesis studies have demonstrated that the hairpin-like structure and hydrophobic cavity are crucial for BrkA passenger domain (virulence effector) translocation. This structure helps in understanding the molecular mechanism of AT assembly and secretion and provides a potential target for anti-pertussis drug design.

PubMed: 21306302
DOI: 10.1042/BJ20101548

Experimental method

X-RAY DIFFRACTION (3 Å)