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Structural insights into the inhibition properties of archaeon citrate synthase from Metallosphaera sedula

机译：结构研究洞爷金属小球藻古柠檬酸合酶的抑制特性

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摘要

Metallosphaera sedula is a thermoacidophilic archaeon and has an incomplete TCA/glyoxylate cycle that is used for production of biosynthetic precursors of essential metabolites. Citrate synthase from M. sedula (MsCS) is an enzyme involved in the first step of the incomplete TCA/glyoxylate cycle by converting oxaloacetate and acetyl-CoA into citrate and coenzyme A. To elucidate the inhibition properties of MsCS, we determined its crystal structure at 1.7 Å resolution. Like other Type-I CS, MsCS functions as a dimer and each monomer consists of two distinct domains, a large domain and a small domain. The oxaloacetate binding site locates at the cleft between the two domains, and the active site was more closed upon binding of the oxaloacetate substrate than binding of the citrate product. Interestingly, the inhibition kinetic analysis showed that, unlike other Type-I CSs, MsCS is non-competitively inhibited by NADH. Finally, amino acids and structural comparison of MsCS with other Type-II CSs, which were reported to be non-competitively inhibited by NADH, revealed that MsCS has quite unique NADH binding mode for non-competitive inhibition.
机译：景天属金属小球菌是嗜热嗜酸古菌，具有不完整的TCA /乙醛酸循环，用于生产必需代谢产物的生物合成前体。贯叶连翘的柠檬酸合酶（MsCS）是将草酰乙酸和乙酰辅酶A转化为柠檬酸和辅酶A的不完全TCA /乙醛酸循环的第一步中涉及的酶。为阐明MsCS的抑制特性，我们确定了其晶体结构分辨率为1.7Å。像其他I型CS一样，MsCS充当二聚体，每个单体都包含两个不同的域，一个大域和一个小域。草酰乙酸酯结合位点位于两个结构域之间的缝隙处，与草酸酯产物的结合相比，草酰乙酸酯底物结合时活性位点更封闭。有趣的是，抑制动力学分析表明，与其他I型CS不同，MsCS被NADH非竞争性抑制。最后，氨基酸和MsCS与其他II型CS的结构比较（据报道被NADH非竞争性抑制）表明，MsCS具有非常独特的NADH结合模式用于非竞争性抑制。

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