The Structure of the Hfq Protein from Chromobacterium haemolyticum Revealed a New Variant of Regulation of RNA Binding with the Protein

IF 0.6 4区材料科学 Q4 CRYSTALLOGRAPHY

Crystallography Reports Pub Date : 2024-02-05 DOI:10.1134/s1063774523600928

N. V. Lekontseva, A. D. Nikulin

引用次数: 0

Abstract

The structure of the Hfq protein from the bacterium Chromobacterium haemolyticum, which forms crystals in two different spatial groups, has been determined. In both cases, the protein has a specific quaternary hexamer-ring structure. The obtained structure showed a previously undescribed interaction between the C-terminal unstructured part of Hfq and the amino acid residues of the proximal RNA-binding site of the protein. This contact may contribute to the regulation of the binding of RNA molecules to the Hfq protein.

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溶血色杆菌 Hfq 蛋白的结构揭示了调节 RNA 与该蛋白结合的新变体

摘要我们测定了溶血色杆菌的 Hfq 蛋白的结构，该蛋白在两个不同的空间群中形成晶体。在这两种情况下，该蛋白质都具有特定的四元六聚环结构。所获得的结构显示，Hfq 的 C 端非结构化部分与该蛋白质近端 RNA 结合位点的氨基酸残基之间存在一种以前未曾描述过的相互作用。这种接触可能有助于调节 RNA 分子与 Hfq 蛋白的结合。

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

Crystallography Reports 化学-晶体学

CiteScore

1.10

自引率

28.60%

发文量

审稿时长

4-8 weeks

期刊介绍： Crystallography Reports is a journal that publishes original articles short communications, and reviews on various aspects of crystallography: diffraction and scattering of X-rays, electrons, and neutrons, determination of crystal structure of inorganic and organic substances, including proteins and other biological substances; UV-VIS and IR spectroscopy; growth, imperfect structure and physical properties of crystals; thin films, liquid crystals, nanomaterials, partially disordered systems, and the methods of studies.

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