Crystallographic characterization of a stress-induced multifunctional protein, rat HBP-23.
HBP-23 is a stress-induced multifunctional rat protein that belongs to a novel family of antioxidant proteins, referred to as peroxiredoxins, and exhibits heme-binding and inhibition of c-Abl protein tyrosine kinase. Recombinant HBP-23 was crystallized by a hanging-drop vapor-diffusion method. The crystals belong to space group P41212 or P43212 with unit-cell dimensions of a = b = 73.47 A, c = 210.37 A and contain two protein molecules in the asymmetric unit. A data set at 2.7-A resolution was collected with a cryo-crystallographic technique. Crystals of selenomethionyl HBP-23 were also obtained under the same conditions.
D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli; D000081062:Heme-Binding Proteins; D006420:Hemeproteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D051381:Rats; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification