Dihydrodipicolinate synthase (DHDPS) from C.jejuni, Y110F mutant with R,R-bislysine bound at the allosteric site at 2.7 Angstrom

Dihydrodipicolinate synthase (DHDPS) from C.jejuni, Y110F mutant with R,R-bislysine bound at the allosteric site at 2.7 Angstrom Descriptor: (2R,5R)-2,5-diamino-2,5-bis(4-aminobutyl)hexanedioic acid, 1,2-ETHANEDIOL, 4-hydroxy-tetrahydrodipicolinate synthase, ... Authors: Saran, S, Sanders, D.A.R. Deposit date: 2021-03-10 Release date: 2022-03-16 Last modified: 2023-10-18 Method: X-RAY DIFFRACTION (2.7 Å) Cite: B-FACTOR ANALYSIS SUGGEST THAT L-LYSINE AND R, R-BISLYSINE ALLOSTERICALLY INHIBIT Cj.DHDPS ENZYME BY DECREASING PROTEIN DYNAMICS To Be Published

空肠弯曲菌（C.jejuni）来源的二氢二吡啶甲酸合酶（Dihydrodipicolinate synthase, DHDPS）Y110F突变体，其别构位点结合R,R-双赖氨酸，结构分辨率为2.7埃。
描述项：(2R,5R)-2,5-二氨基-2,5-双(4-氨基丁基)己二酸、1,2-乙二醇、4-羟基四氢二吡啶甲酸合酶等。
作者：Saran, S、Sanders, D.A.R.
提交日期：2021-03-10
发布日期：2022-03-16
最后修改日期：2023-10-18
实验方法：X射线衍射（分辨率2.7 Å）
引用说明：B因子（B-FACTOR）分析表明，L-赖氨酸与R,R-双赖氨酸可通过降低蛋白质动力学，别构抑制空肠弯曲菌来源的DHDPS酶，该研究成果待发表。