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首页> 外文期刊>Journal of Molecular Biology >Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif
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Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif

机译：当N末端融合到噬菌体T4纤维蛋白折叠三聚体化基序上时，腺病毒纤维轴序列折叠成天然的三倍β螺旋形折叠

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Adenovirus fibres are trimeric proteins that consist of a globular C-terminal domain, a central fibrous shaft and an N-terminal part that attaches to the viral capsid. In the presence of the globular C-terminal domain, which is necessary for correct trimerisation, the shaft segment adopts a triple beta-spiral conformation. We have replaced the head of the fibre by the trimerisation domain of the bacteriophage T4 fibritin, the foldon. Two different fusion constructs were made and crystallised, one with an eight amino acid residue linker and one with a linker of only two residues.X-ray crystallographic studies of both fusion proteins shows that residues 319-391 of the adenovirus type 2 fibre shaft fold into a triple beta-spiral fold indistinguishable from the native structure, although this is now resolved at a higher resolution of 1.9 Angstrom. The foldon residues 458-483 also adopt their natural structure. The intervening linkers are not well ordered in the crystal structures.This work shows that the shaft sequences retain their capacity to fold into their native beta-spiral fibrous fold when fused to a foreign C-terminal trimerisation motif. It provides a structural basis to artificially trimerise longer adenovirus shaft segments and segments from other trimeric beta-structured fibre proteins. Such artificial fibrous constructs, amenable to crystallisation and solution studies, can offer tractable model systems for the study of beta-fibrous structure. They can also prove useful for gene therapy and fibre engineering applications. (C) 2004 Elsevier Ltd. All rights reserved.
机译：腺病毒纤维是三聚体蛋白质，由球状C末端结构域，中央纤维轴和附着于病毒衣壳的N末端部分组成。在正确的三聚化所必需的球状C末端结构域的情况下，轴节采用三重β-螺旋构象。我们已经用噬菌体T4纤维蛋白的三聚结构域，即折叠蛋白代替了纤维的头部。制备并结晶了两种不同的融合构建体，一种具有八个氨基酸残基接头，而一种仅具有两个残基接头。两种融合蛋白的X射线晶体学研究表明，腺病毒2型纤维轴折叠的残基319-391。形成一个与天然结构无法区分的三重β螺旋形折叠，尽管现在可以以1.9埃的更高分辨率进行分辨。折叠残基458-483也采用其天然结构。中间的接头在晶体结构中的排列不是很好。这项工作表明，当与外来的C端三聚化基序融合时，轴序列保留折叠成其天然β-螺旋纤维折叠的能力。它为人为地将更长的腺病毒杆状节段和其他三聚体β结构纤维蛋白的节段提供了结构基础。这种适于结晶和溶液研究的人造纤维构建体可以为研究β-纤维结构提供易于处理的模型系统。它们还可证明对基因治疗和纤维工程应用有用。 （C）2004 Elsevier Ltd.保留所有权利。

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