Investigating the folding pathway and substrate induced conformational changes in B. malayi Guanylate kinase

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• 作者：Smita Gupta^a ; Sunita Yadav^a ; Venkatesan Suryanarayanan^b ; Sanjeev K. Singh^b ; Jitendra K. Saxena^a ; ^{jkscdri@yahoo.com}
• 关键词：NMP kinase ; nucleoside monophosphate kinase ; BmGK ; Brugia malayi Guanylate kinase ; SEC ; Size Exclusion chromatography ; GdnCl ; guanidine hydrochloride ; MS ; molecular simulation
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：94
• 期：part_PA
• 页码：621-633
• 全文大小：3783 K
• 卷排序：94

文摘

Detailed biophysical characterization of BmGK carried out for the first time. Folding pathway of BmGK is altered upon binding of substrates (GMP & ATP). Binding of substrates stabilises BmGK. The binding interaction of Arg145 with GMP shows a switch over to ATP after 40 ns simulation of BmGK-GMP-ATP ternary complex. Addition of ATP also results in increase in fluctuation in BmGK-GMP-ATP complex in the region from 130 to 150 residues.