Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP

Protein Data Bank Japan2023-12-06 更新2026-03-21 收录

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Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP Descriptor: ADENOSINE-5'-DIPHOSPHATE, CARBAMATE KINASE, MAGNESIUM ION Authors: Ramon-Maiques, S, Marina, A, Uriarte, M, Fita, I, Rubio, V. Deposit date: 2000-04-28 Release date: 2000-07-04 Last modified: 2023-12-06 Method: X-RAY DIFFRACTION (1.5 Å) Cite: The 1.5-A Resolution Crystal Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase from the Hyperthermophilic Archaeon Pyrococcus Furiosus, Bound to Adp, Confirms that This Thermoestable Enzyme is a Carbamate Kinase, and Provides Insights Into Substrate Binding and Stability in Carbamate Kinases J.Mol.Biol., 299, 2000

结合腺苷二磷酸（ADP）的超嗜热古菌激烈热球菌（Pyrococcus furiosus）类氨基甲酸酯激酶型氨甲酰磷酸合成酶结构描述项：腺苷-5'-二磷酸、氨基甲酸酯激酶、镁离子作者：Ramon-Maiques S、Marina A、Uriarte M、Fita I、Rubio V 存档日期：2000-04-28 发布日期：2000-07-04 最后修改日期：2023-12-06 检测方法：X射线衍射（1.5埃）引用：《结合腺苷二磷酸的超嗜热古菌激烈热球菌类氨基甲酸酯激酶型氨甲酰磷酸合成酶1.5埃分辨率晶体结构》一文证实，该耐热酶属于氨基甲酸酯激酶家族，其研究结果为阐释氨基甲酸酯激酶的底物结合特性与稳定性机制提供了新视角，刊载于《J. Mol. Biol.》2000年第299卷

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2000-04-28