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Crystal structure of the [(THF)Cs(?-?5:?5-Cp')3Yb] n oligomer.

ABSTRACT: The green compound poly[(tetra-hydro-furan)-tris-[?-?5:?5-1-(tri-methyl-sil-yl)cyclo-penta-dien-yl]caesium(I)ytterbium(II)], [CsYb(C8H13Si)3(C4H8O)] n or [(THF)Cs(?-?5:?5-Cp')3YbII] n was synthesized by reduction of a red THF solution of (C5H4SiMe3)3YbIII with excess Cs metal and identified by X-ray diffraction. The compound crystallizes as a two-dimensional array of hexa-gons with alternating CsI and YbII ions at the vertices and cyclo-penta-dienyl groups bridging each edge. This, based off the six-electron cyclo-penta-dienyl rings occupying three coordination positions, gives a formally nine-coordinate tris-(cyclo-penta-dien-yl) coordination environment to Yb and the Cs is ten-coordinate due to the three cyclo-penta-dienyl rings and a coordinated mol-ecule of THF. The complex comprises layers of Cs3Yb3 hexa-gons with THF ligands and Me3Si groups in between the layers. The Yb-C metrical parameters are consistent with a 4f 14 YbII electron configuration.

SUBMITTER: Huh DN

PROVIDER: S-EPMC7336790 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Crystal structure of the [(THF)Cs(μ-η5:η5-Cp')3Yb] n oligomer.

Huh Daniel N DN Ziller Joseph W JW Evans William J WJ

Acta crystallographica. Section E, Crystallographic communications 20200623 Pt 7

The green compound poly[(tetra-hydro-furan)-tris-[μ-η5:η5-1-(tri-methyl-sil-yl)cyclo-penta-dien-yl]caesium(I)ytterbium(II)], [CsYb(C8H13Si)3(C4H8O)] n or [(THF)Cs(μ-η5:η5-Cp')3YbII] n was synthesized by reduction of a red THF solution of (C5H4SiMe3)3YbIII with excess Cs metal and identif ...[more]

PMID: 32695466

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Project description:BackgroundCrystal structures of the tobacco mosaic virus (TMV) coat protein (CP) in its helical and disk conformations have previously been determined at the atomic level. For the helical structure, interactions of proteins and nucleic acids in the main chains were clearly observed; however, the conformation of residues at the C-terminus was flexible and disordered. For the four-layer aggregate disk structure, interactions of the main chain residues could only be observed through water-mediated hydrogen bonding with protein residues. In this study, the effects of the C-terminal peptides on the interactions of TMV CP were investigated by crystal structure determination.Methodology/principal findingsThe crystal structure of a genetically engineered TMV CP was resolved at 3.06 Å. For the genetically engineered TMV CP, a six-histidine (His) tag was introduced at the N-terminus, and the C-terminal residues 155 to 158 were truncated (N-His-TMV CP(19)). Overall, N-His-TMV CP(19) protein self-assembled into the four-layer aggregate form. The conformations of residues Gln36, Thr59, Asp115 and Arg134 were carefully analyzed in the high radius and low radius regions of N-His-TMV CP(19), which were found to be significantly different from those observed previously for the helical and four-layer aggregate forms. In addition, the aggregation of the N-His-TMV CP(19) layers was found to primarily be mediated through direct hydrogen-bonding. Notably, this engineered protein also can package RNA effectively and assemble into an infectious virus particle.ConclusionThe terminal sequence of amino acids influences the conformation and interactions of the four-layer aggregate. Direct protein-protein interactions are observed in the major overlap region when residues Gly155 to Thr158 at the C-terminus are truncated. This engineered TMV CP is reassembled by direct protein-protein interaction and maintains the normal function of the four-layer aggregate of TMV CP in the presence of RNA.

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Crystal structure of the [(THF)Cs(?-?5:?5-Cp')3Yb] n oligomer.

Publications

Crystal structure of the [(THF)Cs(μ-η<sup>5</sup>:η<sup>5</sup>-Cp')<sub>3</sub>Yb] <sub><i>n</i></sub> oligomer.

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