通过CusF中阳离子-π相互作用和甲硫氨酸相互作用实现的Cu(I)识别
Cu(I) recognition via cation-pi and methionine interactions in CusF.
作者信息
Xue Yi, Davis Anna V, Balakrishnan Gurusamy, Stasser Jay P, Staehlin Benjamin M, Focia Pamela, Spiro Thomas G, Penner-Hahn James E, O'Halloran Thomas V
机构信息
Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.
出版信息
Nat Chem Biol. 2008 Feb;4(2):107-9. doi: 10.1038/nchembio.2007.57. Epub 2007 Dec 23.
Abstract
Methionine-rich motifs have an important role in copper trafficking factors, including the CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-pi interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.
摘要
富含甲硫氨酸的基序在包括CusF蛋白在内的铜转运因子中发挥着重要作用。在此我们表明，CusF利用了一个新的金属识别位点，其中Cu(I)从一个Met2His配体平面沿四方方向朝着一个保守的色氨酸位移。光谱研究表明，硫醚配位以及与色氨酸的强阳离子-π相互作用均能稳定金属结合。这种新型活性位点化学为控制偶然金属的氧化还原和取代化学提供了机制。
相似文献
1
Cu(I) recognition via cation-pi and methionine interactions in CusF.通过CusF中阳离子-π相互作用和甲硫氨酸相互作用实现的Cu(I)识别
Nat Chem Biol. 2008 Feb;4(2):107-9. doi: 10.1038/nchembio.2007.57. Epub 2007 Dec 23.
2
Kβ Valence to Core X-ray Emission Studies of Cu(I) Binding Proteins with Mixed Methionine - Histidine Coordination. Relevance to the Reactivity of the M- and H-sites of Peptidylglycine Monooxygenase.铜（I）结合蛋白与蛋氨酸-组氨酸混合配位的Kβ价层到内层X射线发射研究。与肽基甘氨酸单加氧酶M位点和H位点反应性的相关性。
Inorg Chem. 2016 Apr 4;55(7):3431-9. doi: 10.1021/acs.inorgchem.5b02842. Epub 2016 Mar 11.
3
Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF.色氨酸与铜（I）的π相互作用微调了细菌金属伴侣蛋白CusF的金属结合特性。
J Biol Inorg Chem. 2009 Aug;14(6):905-12. doi: 10.1007/s00775-009-0503-y. Epub 2009 Apr 21.
4
Insight into the cation-π interaction at the metal binding site of the copper metallochaperone CusF.深入了解铜金属伴侣蛋白 CusF 金属结合位点的阳离子-π 相互作用。
J Am Chem Soc. 2011 Dec 7;133(48):19330-3. doi: 10.1021/ja208662z. Epub 2011 Nov 10.
5
Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusF.ATP 酶介导的 Cu+ 外排和递送至周质伴侣的机制：大肠杆菌 CopA 和 CusF 的相互作用。
J Biol Chem. 2014 Jul 25;289(30):20492-501. doi: 10.1074/jbc.M114.577668. Epub 2014 Jun 10.
6
EPR spectroscopy identifies Met and Lys residues that are essential for the interaction between the CusB N-terminal domain and metallochaperone CusF.电子顺磁共振光谱法鉴定出了对于CusB N端结构域与金属伴侣蛋白CusF之间相互作用至关重要的甲硫氨酸（Met）和赖氨酸（Lys）残基。
Metallomics. 2015 Jul;7(7):1163-72. doi: 10.1039/c5mt00053j. Epub 2015 May 5.
7
Models for the Metal Transfer Complex of the N-Terminal Region of CusB and CusF.CusB和CusF N端区域金属转移复合物的模型。
Biochemistry. 2015 Jul 14;54(27):4226-35. doi: 10.1021/acs.biochem.5b00195. Epub 2015 Jul 2.
8
Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy.原子分辨率晶体学和X射线吸收光谱揭示的大肠杆菌CusF不寻常的铜（I）/银（I）配位
Protein Sci. 2007 Oct;16(10):2287-93. doi: 10.1110/ps.073021307.
9
Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone.周质蛋白之间的直接金属转移鉴定出一种细菌铜伴侣蛋白。
Biochemistry. 2008 Nov 4;47(44):11408-14. doi: 10.1021/bi801638m. Epub 2008 Oct 11.
10
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.通过 NMR 光谱和化学交联结合质谱鉴定 CusF 和 CusB 之间的相互作用。
Biochemistry. 2011 Apr 5;50(13):2559-66. doi: 10.1021/bi102012j. Epub 2011 Mar 8.
引用本文的文献
1
Biomimetic Pseudopeptides to Decipher the Interplay between Cu and Methionine-Rich Domains in Proteins.用于解析蛋白质中铜与富含甲硫氨酸结构域之间相互作用的仿生假肽
Chemistry. 2025 Feb 20;31(11):e202403896. doi: 10.1002/chem.202403896. Epub 2025 Jan 9.
2
Mechanisms of Copper Selectivity and Release by the Metallochaperone CusF: Insights from CO-Binding, Rapid-Freeze-Quench EXAFS, and Unnatural Amino Acid Substitution.金属伴侣蛋白 CusF 对铜的选择性和释放机制：来自 CO 结合、快速冷冻淬灭 EXAFS 和非天然氨基酸取代的见解。
Inorg Chem. 2024 Nov 11;63(45):21519-21530. doi: 10.1021/acs.inorgchem.4c03578. Epub 2024 Oct 29.
3
Genetically encoded bioorthogonal tryptophan decaging in living cells.活细胞中基因编码的生物正交色氨酸脱笼反应。
Nat Chem. 2024 Apr;16(4):533-542. doi: 10.1038/s41557-024-01463-7. Epub 2024 Feb 28.
4
The battle for silver binding: How the interplay between the SilE, SilF, and SilB proteins contributes to the silver efflux pump mechanism.争夺银离子结合位：SilE、SilF 和 SilB 蛋白之间的相互作用如何促进了银外排泵机制。
J Biol Chem. 2023 Aug;299(8):105004. doi: 10.1016/j.jbc.2023.105004. Epub 2023 Jul 1.
5
Important Structural Features of Thiolate-Rich Four-Helix Bundles for Cu(I) Uptake and Removal.富含巯基的四螺旋束的重要结构特征及其对 Cu(I) 的摄取和去除。
Inorg Chem. 2023 May 1;62(17):6617-6628. doi: 10.1021/acs.inorgchem.2c04490. Epub 2023 Apr 14.
6
A reinforcement learning approach for protein-ligand binding pose prediction.一种用于蛋白质-配体结合构象预测的强化学习方法。
BMC Bioinformatics. 2022 Sep 8;23(1):368. doi: 10.1186/s12859-022-04912-7.
7
Periplasmic oxidized-protein repair during copper stress in E. coli: A focus on the metallochaperone CusF.铜胁迫下大肠杆菌周质氧化蛋白修复：聚焦金属伴侣蛋白 CusF。
PLoS Genet. 2022 Jul 11;18(7):e1010180. doi: 10.1371/journal.pgen.1010180. eCollection 2022 Jul.
8
Mining anion-aromatic interactions in the Protein Data Bank.在蛋白质数据库中挖掘阴离子-芳香族相互作用。
Chem Sci. 2022 Mar 1;13(14):3984-3998. doi: 10.1039/d2sc00763k. eCollection 2022 Apr 6.
9
Copper monooxygenase reactivity: Do consensus mechanisms accurately reflect experimental observations?铜单加氧酶反应性：共识机制是否准确反映实验观察结果？
J Inorg Biochem. 2022 Jun;231:111780. doi: 10.1016/j.jinorgbio.2022.111780. Epub 2022 Feb 28.
10
Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.通过新型结合位点，细菌外膜蛋白 OprC 摄取离子态铜。
PLoS Biol. 2021 Nov 11;19(11):e3001446. doi: 10.1371/journal.pbio.3001446. eCollection 2021 Nov.
本文引用的文献
1
Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy.原子分辨率晶体学和X射线吸收光谱揭示的大肠杆菌CusF不寻常的铜（I）/银（I）配位
Protein Sci. 2007 Oct;16(10):2287-93. doi: 10.1110/ps.073021307.
2
Periplasmic metal-resistance protein CusF exhibits high affinity and specificity for both CuI and AgI.周质金属抗性蛋白CusF对CuI和AgI均表现出高亲和力和特异性。
Biochemistry. 2006 Sep 19;45(37):11096-102. doi: 10.1021/bi0612622.
3
Intermolecular transfer of copper ions from the CopC protein of Pseudomonas syringae. Crystal structures of fully loaded Cu(I)Cu(II) forms.丁香假单胞菌CopC蛋白中铜离子的分子间转移。完全负载的Cu(I)Cu(II)形式的晶体结构。
J Am Chem Soc. 2006 May 3;128(17):5834-50. doi: 10.1021/ja058528x.
4
A novel copper-binding fold for the periplasmic copper resistance protein CusF.周质铜抗性蛋白CusF的一种新型铜结合折叠结构。
Biochemistry. 2005 Aug 9;44(31):10533-40. doi: 10.1021/bi050827b.
5
A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase.一种可能参与细菌细胞色素c氧化酶CuA中心组装的铜（I）蛋白。
Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3994-9. doi: 10.1073/pnas.0406150102. Epub 2005 Mar 7.
6
Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli.大肠杆菌铜转运外排系统CusCFBA的分子分析。
J Bacteriol. 2003 Jul;185(13):3804-12. doi: 10.1128/JB.185.13.3804-3812.2003.
7
Transition metal speciation in the cell: insights from the chemistry of metal ion receptors.细胞中的过渡金属形态：来自金属离子受体化学的见解
Science. 2003 May 9;300(5621):931-6. doi: 10.1126/science.1085049.
8
A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites.CopC中的氧化还原开关：一种有趣的铜转运蛋白，可在不同位点结合一价铜和二价铜。
Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3814-9. doi: 10.1073/pnas.0636904100. Epub 2003 Mar 21.
9
The PcoC copper resistance protein coordinates Cu(I) via novel S-methionine interactions.PcoC铜抗性蛋白通过新型S-甲硫氨酸相互作用来配位Cu(I)。
J Am Chem Soc. 2003 Jan 15;125(2):342-3. doi: 10.1021/ja028935y.
10
The Cationminus signpi Interaction.阳离子减号π相互作用。
Chem Rev. 1997 Aug 5;97(5):1303-1324. doi: 10.1021/cr9603744.
Zotero 插件