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15N NMR Relaxation Study of the Catalytic Residues in Y14F Mutant Ketosteroid Isomerase

김철|이형주|윤예정|이희천
한국자기공명학회 (Korean Magnetic Resonance Society)|2004.12|Journal of the Korean Magnetic Resonance Society|제8권 제2호|pp. 77-85

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Abstract

1H-detected 15N NMR was employed to investigated the effect of mutation (Y14F) on the dynamic properties of catalytic residues in Δ5-3- ketosteroid isomerase (KSI) from Conamonas testosteroni. In particular, the backbone dynamics of the catalytic residues have been studied in free enzyme and its complex with a steroid ligand, 19-nortestosterone hemisuccinate, by 15N relaxation measurements. The relaxation data were analyzed using the model-free formalism to extract the model-free parameters ( , , and ). The results show that the mutation causes a significant decrease in the order parameter ( ) for the catalytic residues of free Y14F KSI, presumably due to breakdown of the hydrogen bond network by mutation. In addition, the order parameters of Phe-14 and Asp-99 increased slightly upon ligand binding, indicating a slight restriction of the high-frequency (pico- to nanosecond) internal motions of the residues in the complexed Y14F KSI, while the order parameter of Tyr-55 decreased significantly upon ligand binding.

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