Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H59K mutant with pyruvate bound in the active site and L-histidine bound at the allosteric site
收藏Protein Data Bank Japan2023-11-29 更新2026-03-21 收录
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Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H59K mutant with pyruvate bound in the active site and L-histidine bound at the allosteric site Descriptor: 1,2-ETHANEDIOL, 4-hydroxy-tetrahydrodipicolinate synthase, ACETATE ION, ... Authors: Saran, S, Majdi Yazdi, M, Sanders, D.A.R. Deposit date: 2020-10-15 Release date: 2021-10-20 Last modified: 2023-11-29 Method: X-RAY DIFFRACTION (1.89 Å) Cite: Reversing the roles of a crucial hydrogen-bonding pair: a lysine-insensitive mutant of Campylobacter jejuni dihydrodipicolinate synthase, H59K, binds histidine in its allosteric site To be Published
空肠弯曲菌(Campylobacter jejuni, C.jejuni)来源的二氢吡啶二羧酸合成酶(Dihydrodipicolinate synthase, DHDPS)H59K突变体,其活性位点结合丙酮酸,别构位点结合L-组氨酸。
描述符:1,2-乙二醇(1,2-ETHANEDIOL)、4-羟基四氢二吡啶二羧酸合成酶(4-hydroxy-tetrahydrodipicolinate synthase)、乙酸根离子(ACETATE ION)……
作者:Saran, S、Majdi Yazdi, M、Sanders, D.A.R.
提交日期:2020-10-15
发布日期:2021-10-20
最后修改日期:2023-11-29
实验方法:X射线衍射(X-RAY DIFFRACTION),分辨率1.89埃(Å)
引用文献:《逆转关键氢键对的作用:空肠弯曲菌二氢吡啶二羧酸合成酶H59K突变体——一种赖氨酸不敏感型突变体,其别构位点结合组氨酸》,待发表
创建时间:
2020-10-15



