Crystallographic study of a MATE transporter presents a difficult case in structure determination with low-resolution, anisotropic data and crystal twinning.

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 DOI:10.1107/S1399004715016995

J. Symerský, Yi Guo, Jimin Wang, Min Lu

引用次数: 1

Abstract

NorM from Neisseria gonorrhoeae (NorM-NG) belongs to the multidrug and toxic compound extrusion (MATE) family of membrane-transport proteins, which can extrude cytotoxic chemicals across cell membranes and confer multidrug resistance. Here, the structure determination of NorM-NG is described, which had been hampered by low resolution (∼ 4 Å), data anisotropy and pseudo-merohedral twinning. The crystal structure was solved using molecular replacement and was corroborated by conducting a difference Fourier analysis. The NorM-NG structure displays an extracellular-facing conformation, similar to that of NorM-NG bound to a crystallization chaperone. The approaches taken to determine the NorM-NG structure and the lessons learned from this study are discussed, which may be useful for analyzing X-ray diffraction data with similar shortcomings.

查看原文本刊更多论文

在低分辨率、各向异性数据和晶体孪晶的情况下，MATE转运体的晶体学研究在结构确定方面存在困难。

淋病奈瑟菌NorM (NorM- ng)属于多药毒性复合挤出(MATE)膜转运蛋白家族，它可以将细胞毒性化学物质挤出细胞膜并产生多药耐药性。本文描述了NorM-NG的结构测定，该测定曾受到低分辨率(~ 4 Å)、数据各向异性和伪面体孪晶的阻碍。晶体结构用分子置换法求解，并通过差分傅立叶分析加以确证。NorM-NG结构呈现面向细胞外的构象，类似于NorM-NG结合结晶伴侣的构象。本文还讨论了确定NorM-NG结构的方法和从本研究中得到的经验教训，这可能对分析具有类似缺陷的x射线衍射数据有用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Acta Crystallographica Section D: Biological Crystallography 生物-晶体学

自引率

13.60%

发文量

审稿时长

3 months

期刊介绍： Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them. Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged. Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.