Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase
文献类型：期刊论文
| 作者 | Ling, Baoping2; Sun, Min2; Bi, Siwei2; Jing, Zhihong2; Liu, Yongjun1,3 |
| 刊名 | journal of molecular graphics & modelling
 |
| 出版日期 | 2012-05-01 |
| 卷号 | 35页码:1-10 |
| 关键词 | L-Alanine dehydrogenase Mycobacterium tuberculosis Principle component analysis Free energy landscape Molecular dynamics simulations |
| ISSN号 | 1093-3263 |
| 中文摘要 | 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. |
| 英文摘要 | 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. |
| WOS标题词 | science & technology ; life sciences & biomedicine ; technology ; physical sciences |
| 类目[WOS] | biochemical research methods ; biochemistry & molecular biology ; computer science, interdisciplinary applications ; crystallography ; mathematical & computational biology |
| 研究领域[WOS] | biochemistry & molecular biology ; computer science ; crystallography ; mathematical & computational biology |
| 关键词[WOS] | bacillus-subtilis ; hyaluronan lyase ; domain motions ; protein ; mechanism ; binding ; purification ; flexibility ; complexes ; antigen |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000304513400001 |
| 公开日期 | 2013-03-15 |
| 源URL | [http://ir.nwipb.ac.cn/handle/363003/3672]  |
| 专题 | 西北高原生物研究所_中国科学院西北高原生物研究所 |
| 作者单位 | 1.Chinese Acad Sci, NW Inst Plateau Biol, Xining 810001, Qinghai, Peoples R China 2.Qufu Normal Univ, Sch Chem & Chem Engn, Qufu 273165, Shandong, Peoples R China 3.Shandong Univ, Sch Chem & Chem Engn, Jinan 250100, Shandong, Peoples R China |
| 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,2012,35:1-10. |
| 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,35,1-10. |
| 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 35(2012):1-10. |
入库方式： OAI收割
来源：西北高原生物研究所
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