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来自布氏锥虫的动基体动粒蛋白KKT23的乙酰转移酶结构域的H、C和N共振归属

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

作者信息

Ludzia Patryk, Nugent Charlotte, Akiyoshi Bungo, Redfield Christina

机构信息

Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.

Department of Biochemistry, University of Cambridge, Cambridge, CB2 1GA, UK.

出版信息

Biomol NMR Assign. 2025 Jun;19(1):187-194. doi: 10.1007/s12104-025-10235-4. Epub 2025 May 2.

Abstract

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 H, C and N resonance assignments for the C-terminal region of KKT23 (KKT23) 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.

摘要

KKT23是一种动基体特异性着丝粒蛋白,其具有一个C端GCN5相关组蛋白乙酰转移酶结构域,可使组蛋白H2A的C端尾部发生乙酰化。在此,我们给出了来自布氏锥虫的KKT23(KKT23)C端区域与已知乙酰转移酶辅因子乙酰辅酶A和辅酶A形成复合物的氢、碳和氮共振归属。这些归属为详细研究溶液中KKT23的结构、动力学和相互作用提供了起点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/062c/12116700/f708f75fc4d2/12104_2025_10235_Fig1_HTML.jpg

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