Dihydrodipicolinate synthase (DHDPS) from C.jejuni with pyruvate bound in the active site and R,R-bislysine bound at the allosteric site in C2221 space group

Dihydrodipicolinate synthase (DHDPS) from C.jejuni with pyruvate bound in the active site and R,R-bislysine bound at the allosteric site in C2221 space group 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: 2020-12-03 Release date: 2021-12-08 Last modified: 2023-11-29 Method: X-RAY DIFFRACTION (1.94 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），其活性位点结合丙酮酸，别构位点结合R,R-双赖氨酸，晶体所属空间群为C2221。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.。提交入库日期：2020-12-03；发布日期：2021-12-08；最后更新日期：2023-11-29。实验方法：X射线衍射（分辨率1.94埃）。引用说明：B因子分析表明，L-赖氨酸与R,R-双赖氨酸可通过降低蛋白质动力学特性别构抑制空肠弯曲菌来源的DHDPS酶，相关研究待发表。