An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of wild-type MopE to 1.35AA

An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of wild-type MopE to 1.35AA Descriptor: CALCIUM ION, COPPER (II) ION, SURFACE-ASSOCIATED PROTEIN Authors: Helland, R, Fjellbirkeland, A, Karlsen, O.A, Ve, T, Lillehaug, J.R, Jensen, H.B. Deposit date: 2008-02-22 Release date: 2008-03-18 Last modified: 2024-10-23 Method: X-RAY DIFFRACTION (1.35 Å) Cite: An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus Capsulatus-Secreted Protein Mope. J.Biol.Chem., 283, 2008

氧化色氨酸可促进荚膜甲基球菌（Methylococcus capsulatus）分泌蛋白MopE的铜结合能力。野生型MopE的结构分辨率为1.35埃，相关描述项：钙离子、铜(II)离子、表面结合蛋白。作者：Helland R、Fjellbirkeland A、Karlsen O.A、Ve T、Lillehaug J.R、Jensen H.B。提交日期：2008-02-22；发布日期：2008-03-18；最后修改日期：2024-10-23。实验方法：X射线衍射（分辨率1.35 Å）。引用文献：《氧化色氨酸促进荚膜甲基球菌分泌蛋白MopE的铜结合能力》，《生物化学杂志》（J. Biol. Chem.），283卷，2008年。