Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum.

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2004-04-01 DOI:10.1107/S0907444904004998

M. Maher, Maddalena Cross, M. Wilce, J. Guss, A. G. Wedd

引用次数: 13

Abstract

Five different metal-substituted forms of Clostridium pasteurianum rubredoxin have been prepared and crystallized. The single Fe atom present in the Fe(S-Cys)(4) site of the native form of the protein was exchanged in turn for Co, Ni, Ga, Cd and Hg. All five forms of rubredoxin crystallized in space group R3 and were isomorphous with the native protein. The Co-, Ni- and Ga-substituted proteins exhibited metal sites with geometries similar to that of the Fe form (effective D(2d) local symmetry), as did the Cd and Hg proteins, but with a significant expansion of the metal-sulfur bond lengths. A knowledge of these structures contributes to a molecular understanding of the function of this simple iron-sulfur electron-transport protein.

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巴氏梭菌红霉素的金属取代衍生物。

制备并结晶了五种不同的金属取代形式的巴氏梭菌红霉素。存在于天然蛋白的Fe(S-Cys)(4)位点上的单个Fe原子依次被Co、Ni、Ga、Cd和Hg交换。所有五种形式的红氧还蛋白都在R3空间群中结晶，并且与天然蛋白同构。Co, Ni和ga取代的蛋白质显示出与Fe形式相似的几何形状的金属位点(有效的D(2d)局部对称)，Cd和Hg蛋白质也是如此，但金属-硫键长度显着扩大。对这些结构的了解有助于对这种简单的铁硫电子传递蛋白的功能进行分子理解。

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 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.