Arginine 116 stabilizes the entrance to the metal ion-binding site of the MntC protein

机译：精氨酸116稳定MntC蛋白的金属离子结合位点的入口

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The cyanobacterium Synechocystis sp. PCC 6803 imports Mn²⁺ ions via MntCAB, an ABC transport system that is expressed at submicromolar Mn²⁺ concentrations. The structures of the wild type (WT) and a site-directed mutant of the MntC solute-binding protein have been determined at 2.7 and 3.5 Å resolution, respectively. The WT structure is significantly improved over the previously determined structure (PDB entry ), showing improved Mn²⁺ binding site parameters, disulfide bonds in all three monomers and ions bound to the protein surface, revealing the role of Zn²⁺ ions in the crystallization liquor. The structure of MntC reveals that the active site is surrounded by neutral-to-positive electrostatic potential and is dominated by a network of polar interactions centred around Arg116. The mutation of this residue to alanine was shown to destabilize loops in the entrance to the metal-ion binding site and suggests a possible role in MntC function.

机译：蓝藻集胞藻PCC 6803通过MntCAB导入Mn ^{2 + 离子，MntCAB是一种以亚微摩尔Mn ^{2 + 浓度表达的ABC转运系统。 MntC溶质结合蛋白的野生型（WT）和定点突变体的结构分别以2.7和3.5Å的分辨率测定。与先前确定的结构（PDB条目）相比，WT结构得到了显着改善，显示出改善的Mn ^{2 + 结合位点参数，所有三个单体中的二硫键以及与蛋白质表面结合的离子，从而揭示了结晶液中的Zn ^{2 + 离子。 MntC的结构表明，该活性位点被中性到正静电势包围，并且被以Arg116为中心的极性相互作用网络所支配。该残基向丙氨酸的突变显示出使金属离子结合位点入口处的环不稳定，并暗示了其在MntC功能中的可能作用。}}}}

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期刊名称 Acta Crystallographica Section F: Structural Biology and Crystallization Communications
作者
Margarita Kanteev; Noam Adir;
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作者单位

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年(卷),期 2013(69),Pt 3
年度 2013
页码 237–242
总页数 6
原文格式 PDF
正文语种
中图分类分子生物学;生化遗传学;生化药理学;生物物理学;
关键词
ABC transporter site-directed mutagenesis cyanobacteria;

机译：ABC转运蛋白;定点诱变;蓝细菌;

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专利

1. Arginine 116 stabilizes the entrance to the metal ion-binding site of the MntC protein [J] . Kanteev Margarita, Adir Noam Acta crystallographica, Section F. Structural biology and crystallization communications . 2013,第3期

机译：精氨酸116稳定MntC蛋白金属离子结合位点的入口
2. MIonSite: Ligand-specific prediction of metal ion-binding sites via enhanced AdaBoost algorithm with protein sequence information [J] . Qiao Liang, Xie Dongqing Analytical Biochemistry: An International Journal of Analytical and Preparative Methods . 2019,第期

机译：MIONSITE：通过增强的Adaboost算法具有蛋白质序列信息的金属离子结合位点的配体特异性预测
3. Flexible aspartates propel iron to the ferroxidation sites along pathways stabilized by a conserved arginine in Dps proteins from Mycobacterium smegmatis [J] . Metallomics. integrated biometal science . 2017,第6期

机译：柔性天冬氨酸沿着来自分枝杆菌的DPS蛋白质中的保守精氨酸稳定的途径将熨斗延伸到铁氧化位点
4. Mn~(2+) Sites Investigated by Advanced EPR Techniques: In-Depth Study of Mn~(2+) Ion-Binding Sites in the Hammerhead Ribozyme [C] . Matthew Vogt, Victoria J. DeRose, American Chemical Society, American Chemical Society national meeting . 2003

机译：通过先进的EPR技术研究了Mn〜（2+）位点：深入研究锤头核苷中的Mn〜（2+）离子结合位点
5. THE RESTRICTION ENDONUCLEASE ECO RI: ITS INTRINSIC METAL CENTER AND SPECIFIC INTERACTIONS WITH A DNA RECOGNITION SITE (PROTEIN-NUCLEIC ACID, ZINC METALLOENZYMES, INTERACTIONS CHIRAL METAL COMPLEXES, DNA-BINDING PROTEINS). [D] . PARANAWITHANA, SHANTHI R. 1986

机译：限制性内切酶Eco RI：其内在金属中心以及与DNA识别位点的特定相互作用（蛋白-核酸，锌金属酶，相互作用的手性金属络合物，DNA结合蛋白）。
6. The α-Subunit Regulates Stability of the Metal Ion at the Ligand-associated Metal Ion-binding Site in β3 Integrins [O] . Xianliang Rui, Mehrdad Mehrbod, Johannes F. Van Agthoven, 2014

机译：α亚基调节β3整联蛋白配体相关金属离子结合位点上金属离子的稳定性。
7. Arginine 116 stabilizes the entrance to the metal ion-binding site of the MntC protein [O] . Margarita Kanteev, Noam Adir 2013

机译：精氨酸116稳定了锰蛋白的金属离子结合位点的入口

Arginine 116 stabilizes the entrance to the metal ion-binding site of the MntC protein

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