The folate‐binding module of Thermus thermophilus Thermus thermophilus cobalamin‐dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'

Yamada Kazuhiro; Koutmos Markos

首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >The folate‐binding module of Thermus thermophilus Thermus thermophilus cobalamin‐dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'

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The folate‐binding module of Thermus thermophilus Thermus thermophilus cobalamin‐dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'

机译：叶酸量绑定模块栖热菌属的酸奶蛋氨酸合成酶显示一个明显的变化古典蒂姆桶:蒂姆桶的“扭曲”

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Methyl transfer between methyltetrahydrofolate and corrinoid molecules is a key reaction in biology that is catalyzed by a number of enzymes in many prokaryotic and eukaryotic organisms. One classic example of such an enzyme is cobalamin‐dependent methionine synthase (MS). MS is a large modular protein that utilizes an S N 2‐type mechanism to catalyze the chemically challenging methyl transfer from the tertiary amine (N5) of methyltetrahydrofolate to homocysteine in order to form methionine. Despite over half a century of study, many questions remain about how folate‐dependent methyltransferases, and MS in particular, function. Here, the structure of the folate‐binding (Fol) domain of MS from Thermus thermophilus is reported in the presence and absence of methyltetrahydrofolate. It is found that the methyltetrahydrofolate‐binding environment is similar to those of previously described methyltransferases, highlighting the conserved role of this domain in binding, and perhaps activating, the methyltetrahydrofolate substrate. These structural studies further reveal a new distinct and uncharacterized topology in the C‐terminal region of MS Fol domains. Furthermore, it is found that in contrast to the canonical TIM‐barrel β 8 α 8 fold found in all other folate‐binding domains, MS Fol domains exhibit a unique β 8 α 7 fold. It is posited that these structural differences are important for MS function.

机译：甲基methyltetrahydrofolate之间转移corrinoid分子生物学中是一个关键的反应催化的酶在许多原核和真核生物。这种酶的例子是外源因素的依赖蛋氨酸合成酶(女士)。蛋白质,利用一个S N 2类型的机制催化化学有挑战性的甲基传输的叔胺(它们)methyltetrahydrofolate同型半胱氨酸在秩序蛋氨酸。的研究中,如何还存在许多问题叶酸高依赖的甲基转移酶和女士具体来说,功能。叶酸量绑定(符合)域的女士从栖热菌属酸奶是在存在和报道缺乏methyltetrahydrofolate。, methyltetrahydrofolate绑定环境是相似的描述甲基转移酶,凸显了在绑定守恒这个领域的作用,methyltetrahydrofolate也许激活衬底。揭示了一个新的不同的和无特征拓扑C检测终端地区的女士指出域。对比规范蒂姆8桶βα8折发现在所有其他叶酸量绑定域名,女士指出8领域表现出一种独特的βα7折。这些结构上的差异女士的重要功能。

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《Acta crystallographica. Section D, Structural biology.》 |2018年第1期|41-51|共10页
作者
Yamada Kazuhiro; Koutmos Markos;
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Department of Chemistry, University of Michigan, Ann Arbor, Michigan, USA;

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正文语种英语
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SCROLL; Multiple Sclerosis; Vitamin B 12Thermus thermophilusFolatetelecommunication interchange markupCobalaminARHGEF5 geneMass spectroscopyTIMELESS gene5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase;

机译：滚动,多发性硬化症,维生素B 12栖热菌属thermophilusFolatetelecommunication交换markupCobalaminARHGEF5 geneMassspectroscopyTIMELESSgene5-Methyltetrahydrofolate-HomocysteineS-Methyltransferase;

The folate‐binding module of Thermus thermophilus Thermus thermophilus cobalamin‐dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'

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