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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: Role of ATP complexation and the glutaminase domain in catalytic coupling
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Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: Role of ATP complexation and the glutaminase domain in catalytic coupling

机译：Formylglycinamide核苷酸amidotransferase鼠伤寒沙门氏菌:ATP的角色络合和谷氨酰胺酶域催化耦合

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摘要

Formylglycinamide ribonucleotide (FGAR) amidotransferase (FGAR-AT) takes part in purine biosynthesis and is a multidomain enzyme with multiple spatially separated active sites. FGAR-AT contains a glutaminase domain that is responsible for the generation of ammonia from glutamine. Ammonia is then transferred via a channel to a second active site located in the synthetase domain and utilized to convert FGAR to formylglycinamidine ribonucleotide (FGAM) in an adenosine triphosphate (ATP) dependent reaction. In some ammonia-channelling enzymes ligand binding triggers interdomain signalling between the two diverse active centres and also assists in formation of the ammonia channel. Previously, the structure of FGAR-AT from Salmonella typhimurium containing a glutamyl thioester intermediate covalently bound in the glutaminase active site was determined. In this work, the roles played by various ligands of FGAR-AT in inducing catalytic coupling are investigated. Structures of FGAR-AT from S. typhimurium were determined in two different states: the unliganded form and the binary complex with an ATP analogue in the presence of the glutamyl thioester intermediate. The structures were compared in order to decipher the roles of these two states in interdomain communication. Using a process of elimination, the results indicated that binding of FGAR is most likely to be the major mechanism by which catalytic coupling occurs. This is because conformational changes do not occur either upon formation of the glutamyl thioester intermediate or upon subsequent ATP complexation. A model of the FGAR-bound form of the enzyme suggested that the loop in the synthetase domain may be responsible for initiating catalytic coupling via its inter-action with the N-terminal domain.
机译：Formylglycinamide核苷酸(FGAR)amidotransferase (FGAR-AT)参加嘌呤生物合成,是一种多畴的酶多个活动的空间上分开。FGAR-AT包含一个谷氨酰胺酶域负责生成氨谷氨酰胺。第二个活性部位位于频道合成酶FGAR转换域和利用formylglycinamidine核苷酸(FGAM)三磷酸腺苷(ATP)的反应。在一些ammonia-channelling酶配体绑定触发interdomain信号之间两个不同的活动中心,还协助氨形成的通道。FGAR-AT从沙门氏菌的结构沙门氏菌感染含有谷酰基硫代酸酯中间谷氨酰胺酶的共价结合活性部位。角色扮演的各种FGAR-AT的配体诱导催化耦合研究。FGAR-AT结构从美国沙门氏菌感染决定在两种不同的状态:unliganded和复杂的二进制形式ATP模拟谷酰基的存在硫代酸酯的中间体。而为了破译的角色两个国家在interdomain沟通。消除的过程,结果显示绑定的FGAR是最有可能的催化耦合的主要机制发生。不是发生在谷酰基的形成硫代酸酯中间或在随后的ATP络合。这种酶建议的循环合成酶域可能负责开始通过其催化耦合与n端结构域相互作用。

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