Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10750827 | Biochemical and Biophysical Research Communications | 2015 | 5 Pages |
Abstract
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 1.50Â Ã
. The crystals belong to space group C2 with unit cell parameters a = 127.1 Ã
, b = 77.3 Ã
, c = 131.6 Ã
, 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.
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Authors
Chunmao Zhang, You Yu, Maojun Yang, Yongqiang Jiang,