The structure of glucose-1-phosphate thymidylyltransferase from Mycobacterium tuberculosis reveals the location of an essential magnesium ion in the RmlA-type enzymes.

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第一作者： Haley A,Brown

第一单位： Department of Biochemistry, University of Wisconsin, Madison, WI, 53706, USA.

作者： Haley A,Brown ^[1] ; James B,Thoden ^[1] ; Peter A,Tipton ^[2] ; Hazel M,Holden ^[1]

作者单位： Department of Biochemistry, University of Wisconsin, Madison, WI, 53706, USA. ^[1] Department of Biochemistry, University of Missouri, Columbia, MO, 65211, USA. ^[2]

关键词 Mycobacterium tuberculosis X-ray crystallography dTDP-l-rhamnose glucose-1-phosphate thymidylyltransferase tuberculosis

主题词别构部位(Allosteric Site);细菌蛋白质类(Bacterial Proteins);结晶学, X线(Crystallography, X-Ray);葡萄糖(Glucose);镁(Magnesium);模型, 分子(Models, Molecular);结核分枝杆菌(Mycobacterium tuberculosis);核苷酸基转移酶类(Nucleotidyltransferases);蛋白质结合(Protein Binding);蛋白质构象(Protein Conformation);胸腺嘧啶核苷酸类(Thymine Nucleotides)

DOI 10.1002/pro.3333

PMID 29076563

发布时间 2019-02-01

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Protein science

2018年27卷2期

441-450页

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The structure of glucose-1-phosphate thymidylyltransferase from Mycobacterium tuberculosis reveals the location of an essential magnesium ion in the RmlA-type enzymes.

Protein science

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Protein science

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The structure of glucose-1-phosphate thymidylyltransferase from Mycobacterium tuberculosis reveals the location of an essential magnesium ion in the RmlA-type enzymes.

Protein science

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Protein science

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