Expression, purification, crystallization and structure determination of the N terminal domain of Fhb, a factor H binding protein from Streptococcus suis.
Fhb is a surface virulence protein from Streptococcus suis, which could aid bacterial evasion of host innate immune defense by recruiting complement regulator factor H to inactivate C3b deposited on bacterial surface in blood. Here we successfully expressed and purified the N terminal domain of Fhb (N-Fhb) and obtained crystals of the N-Fhb by sitting-drop vapor diffusion method with a resolution of 1.50 Å. The crystals belong to space group C2 with unit cell parameters a = 127.1 Å, b = 77.3 Å, c = 131.6 Å, α = 90°, β = 115.9°, γ = 90°. The structure of N-Fhb was determined by SAD method and the core structure of N-Fhb is a β sandwich. We speculated that binding of Fhb to human factor H may be mainly mediated by surface amino acids with negative charges.
['Zhang|Chunmao|C|', 'Yu|You|Y|', 'Yang|Maojun|M|', 'Jiang|Yongqiang|Y|']
D000818:Animals D001426:Bacterial Proteins D002352:Carrier Proteins D017242:Complement Factor H D003460:Crystallization D018360:Crystallography, X-Ray D006801:Humans D057131:Immune Evasion D007113:Immunity, Innate D008958:Models, Molecular D017434:Protein Structure, Tertiary D011994:Recombinant Proteins D055672:Static Electricity D017011:Streptococcus suis D014774:Virulence
Fhb Streptococcus suis β sandwich Negative charges Crystal structure