Nucleotide-bound crystal structures of the SARS-CoV-2 helicase NSP13.

IF 1.1 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Acta crystallographica. Section F, Structural biology communications Pub Date : 2025-08-01 Epub Date: 2025-07-10 DOI:10.1107/S2053230X25005266

Patrick Kloskowski, Piotr Neumann, Annette Berndt, Ralf Ficner

引用次数: 0

Abstract

Nucleotide-bound crystal structures of SARS-CoV-2 NSP13 in ADP- and ATP-bound states were resolved to 1.8 and 1.9 Å, respectively. The ADP-bound model captures a state immediately following ATP hydrolysis, with both ADP and orthophosphate still present in the active site. Further comparative analysis revealed that crystal packing influences NSP13 by stabilizing the nucleotide-binding site, underscoring the importance of accounting for these effects in structure-based drug design targeting NSP13.

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SARS-CoV-2解旋酶NSP13的核苷酸结合晶体结构

SARS-CoV-2 NSP13在ADP和atp结合状态下的核苷酸结合晶体结构分别分解为1.8和1.9 Å。ADP结合模型在ATP水解后立即捕获状态，ADP和正磷酸盐仍然存在于活性位点。进一步的比较分析表明，晶体包装通过稳定核苷酸结合位点来影响NSP13，强调了在基于结构的药物设计中考虑这些效应的重要性。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Acta crystallographica. Section F, Structural biology communications BIOCHEMICAL RESEARCH METHODSBIOCHEMISTRY &-BIOCHEMISTRY & MOLECULAR BIOLOGY

CiteScore

1.90

自引率

0.00%

发文量

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.