时间分辨串行同步辐射晶体学揭示的衣藻 LOV1 结构。

IF 2.9 2区材料科学 Q2 CHEMISTRY, MULTIDISCIPLINARY

IUCrJ Pub Date : 2024-09-01 DOI:10.1107/S2052252524008327

Marius Schmidt

引用次数: 0

摘要

室温时间分辨串行晶体学研究了衣藻趋光蛋白 LOV1 结构域的光反应。中心黄素单核苷酸发色团的 C4a 原子与蛋白质半胱氨酸之间形成了共价加合物。该加合物的结构与 23 年前从麦冬蕨类植物 Phy3 中测定的 LOV2 的结构非常相似。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文本刊更多论文

The structure of Chlamydomonas LOV1 as revealed by time-resolved serial synchrotron crystallography

The photo-reaction of the LOV1 domain of the Chlamydomonas reinhardtii phototropin is investigated by room-temperature time-resolved serial crystallography. A covalent adduct forms between the C4a atom of the central flavin-mononucleotide chromophore and a protein cysteine. The structure of the adduct is very similar to that of LOV2 determined 23 years ago from the maidenhair fern Phy3.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

IUCrJ CHEMISTRY, MULTIDISCIPLINARYCRYSTALLOGRAPH-CRYSTALLOGRAPHY

CiteScore

7.50

自引率

5.10%

发文量

审稿时长

10 weeks

期刊介绍： IUCrJ is a new fully open-access peer-reviewed journal from the International Union of Crystallography (IUCr). The journal will publish high-profile articles on all aspects of the sciences and technologies supported by the IUCr via its commissions, including emerging fields where structural results underpin the science reported in the article. Our aim is to make IUCrJ the natural home for high-quality structural science results. Chemists, biologists, physicists and material scientists will be actively encouraged to report their structural studies in IUCrJ.