Crystal structure of the accessory translocation ATPase, SecA2, from Clostridium difficile, in complex with adenosine-5'-(gamma-thio)-triphosphate

Crystal structure of the accessory translocation ATPase, SecA2, from Clostridium difficile, in complex with adenosine-5'-(gamma-thio)-triphosphate Descriptor: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, Protein translocase subunit SecA 2 Authors: Lindic, N, Loboda, J, Usenik, A, Turk, D. Deposit date: 2019-10-14 Release date: 2020-11-18 Last modified: 2024-01-31 Method: X-RAY DIFFRACTION (2.9 Å) Cite: The Structure of Clostridioides difficile SecA2 ATPase Exposes Regions Responsible for Differential Target Recognition of the SecA1 and SecA2-Dependent Systems. Int J Mol Sci, 21, 2020

艰难梭菌（Clostridioides difficile）附属易位ATP酶SecA2与腺苷-5'-γ-硫代三磷酸（adenosine-5'-(gamma-thio)-triphosphate）形成复合物的晶体结构。描述符：硫代磷酸腺苷酯（PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER）、蛋白质易位亚基SecA2。作者：Lindic, N、Loboda, J、Usenik, A、Turk, D。保藏日期：2019-10-14；发布日期：2020-11-18；最后修改日期：2024-01-31。实验方法：X射线衍射（X-RAY DIFFRACTION），分辨率2.9埃（Å）。引用文献：《艰难梭菌SecA2 ATP酶的结构揭示了介导SecA1与SecA2依赖系统差异化靶标识别的区域》，刊载于《国际分子科学杂志》（Int J Mol Sci），2020年，第21卷。