分辨率为 1.38 Å 的人组氨酸三核苷酸结合蛋白 1 (hHINT1) 与 5'- 磷酸腺苷复合物的新晶体形态。

Rafał Dolot, Magdalena Ozga, Artur Włodarczyk, Agnieszka Krakowiak, Barbara Nawrot
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引用次数: 0

摘要

组氨酸三聚体核苷酸结合蛋白 1(HINT1)是组氨酸三聚体蛋白超家族中最古老、最广泛的分支。HINT1 在多种生物过程中发挥着重要作用,在许多物种中都有发现。本文报告了从一种新的单斜晶体中获得的分辨率为 1.38 Å 的人类 HINT1 腺苷-5'-单磷酸(AMP)复合物结构。最终结构的 R(cryst) = 0.1207(R(free) = 0.1615),模型具有良好的立体化学质量。对高分辨率数据的详细分析使得蛋白质结构的细节与之前公布的数据相比得到了更新。
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A new crystal form of human histidine triad nucleotide-binding protein 1 (hHINT1) in complex with adenosine 5'-monophosphate at 1.38 Å resolution.

Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch of the histidine triad protein superfamily. HINT1 plays an important role in various biological processes and has been found in many species. Here, the structure of the human HINT1-adenosine 5'-monophosphate (AMP) complex at 1.38 Å resolution obtained from a new monoclinic crystal form is reported. The final structure has R(cryst) = 0.1207 (R(free) = 0.1615) and the model exhibits good stereochemical quality. Detailed analysis of the high-resolution data allowed the details of the protein structure to be updated in comparison to the previously published data.

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期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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