布鲁氏锥虫着丝粒蛋白KKT23乙酰转移酶结构域的1H， 13C和15N共振分配。

IF 0.6 4区生物学 Q4 BIOPHYSICS

Biomolecular NMR Assignments Pub Date : 2025-05-02 DOI:10.1007/s12104-025-10235-4

Patryk Ludzia, Charlotte Nugent, Bungo Akiyoshi, Christina Redfield

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引用次数: 0

摘要

KKT23是一种着丝质体特异性的着丝粒蛋白，具有c端gcn5相关的组蛋白乙酰转移酶结构域，可使组蛋白H2A的c端尾部乙酰化。在这里，我们给出了来自布氏锥虫的KKT23 （KKT23125-348）的c端区域与已知的乙酰转移酶、乙酰辅酶A和辅酶A的辅因子的1H、13C和15N共振赋值，这些赋值为详细研究KKT23在溶液中的结构、动力学和相互作用提供了起点。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

1H, 13C and 15N resonance assignments for the acetyltransferase domain of the kinetoplastid kinetochore protein KKT23 from Trypanosoma brucei

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1H, 13C and 15N resonance assignments for the acetyltransferase domain of the kinetoplastid kinetochore protein KKT23 from Trypanosoma brucei

KKT23 is a kinetoplastid-specific kinetochore protein that has a C-terminal GCN5-related histone acetyltransferase domain that acetylates the C-terminal tail of histone H2A. Here, we present the ¹H, ¹³C and ¹⁵N resonance assignments for the C-terminal region of KKT23 (KKT23^125–348) from Trypanosoma brucei in complex with known cofactors for acetyltransferases, acetyl coenzyme A and coenzyme A. These assignments provide the starting point for detailed investigation of the structure, dynamics and interactions of KKT23 in solution.

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来源期刊

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.