Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase

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	Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase
	Ling, Baoping ; Sun, Min ; Bi, Siwei ; Jing, Zhihong ; Liu, Yongjun
	2012-05-01
发表期刊	JOURNAL OF MOLECULAR GRAPHICS & MODELLING ; Wang, JH; Sheng, X; Zhao, Y; Liu, YJ; Liu, CB.Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase,JOURNAL OF MOLECULAR GRAPHICS & MODELLING,2012,35():1-10
摘要	Mycobacterium tuberculosis L-alanine dehydrogenase (L-MtAlaDH) catalyzes the NADH-dependent reversible oxidative deamination of t-alanine to pyruvate and ammonia. L-MtAlaDH has been proposed to be a potential target in the treatment of tuberculosis. Based on the crystal structures of this enzyme, molecular dynamics simulations were performed to investigate the conformational changes of L-MtAlaDH induced by coenzyme NADH. The results show that the presence of NADH in the binding domain restricts the motions and conformational distributions of L-MtAlaDH. There are two loops (residues 94-99 and 238-251) playing important roles for the binding of NADH, while another loop (residues 267-293) is responsible for the binding of substrate. The opening/closing and twisting motions of two domains are closely related to the conformational changes of L-MtAlaDH induced by NADH. (C) 2012 Elsevier Inc. All rights reserved.; Mycobacterium tuberculosis L-alanine dehydrogenase (L-MtAlaDH) catalyzes the NADH-dependent reversible oxidative deamination of t-alanine to pyruvate and ammonia. L-MtAlaDH has been proposed to be a potential target in the treatment of tuberculosis. Based on the crystal structures of this enzyme, molecular dynamics simulations were performed to investigate the conformational changes of L-MtAlaDH induced by coenzyme NADH. The results show that the presence of NADH in the binding domain restricts the motions and conformational distributions of L-MtAlaDH. There are two loops (residues 94-99 and 238-251) playing important roles for the binding of NADH, while another loop (residues 267-293) is responsible for the binding of substrate. The opening/closing and twisting motions of two domains are closely related to the conformational changes of L-MtAlaDH induced by NADH. (C) 2012 Elsevier Inc. All rights reserved.
文献类型	期刊论文
条目标识符	http://210.75.249.4/handle/363003/41977
专题	中国科学院西北高原生物研究所
推荐引用方式 GB/T 7714	Ling, Baoping,Sun, Min,Bi, Siwei,et al. Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase[J]. JOURNAL OF MOLECULAR GRAPHICS & MODELLING, Wang, JH; Sheng, X; Zhao, Y; Liu, YJ; Liu, CB.Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase,JOURNAL OF MOLECULAR GRAPHICS & MODELLING,2012,35():1-10,2012.
APA	Ling, Baoping,Sun, Min,Bi, Siwei,Jing, Zhihong,&Liu, Yongjun.(2012).Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase.JOURNAL OF MOLECULAR GRAPHICS & MODELLING.
MLA	Ling, Baoping,et al."Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase".JOURNAL OF MOLECULAR GRAPHICS & MODELLING (2012).