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Báo cáo khoa học: Large conformational changes in the Escherichia coli tryptophan synthase b2 subunit upon pyridoxal 5¢-phosphate binding
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To understand the basis for the lower activity of the tryptophan synthaseb2 subunit in comparison to thea2b2 complex, we determined the crystal struc-tures of apo-b2 and holo-b2 from Escherichia coliat 3.0 and 2.9 A˚ resolu-tions, respectively. To our knowledge, this is the first report of both b2 subunit structures with and without pyridoxal-5¢-phosphate.
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