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来自聚球藻的[2Fe-2S]铁氧化还原蛋白I在2.5埃分辨率下的主链折叠。

Main chain fold of a [2Fe-2S]ferredoxin I from Aphanothece sacrum at 2.5 A resolution.

作者信息

Tsutsui T, Tsukihara T, Fukuyama K, Katsube Y, Hase T, Matsubara H, Nishikawa Y, Tanaka N

出版信息

J Biochem. 1983 Jul;94(1):299-302. doi: 10.1093/oxfordjournals.jbchem.a134343.

Abstract

Crystal structure analysis of a [2Fe-2S]ferredoxin I from Aphanothece sacrum, a blue green alga, was carried out at 2.5 A resolution. The phase angle of each reflection was determined by the single isomorphous replacement method coupled with the anomalous dispersion effect for the uranium derivative. The four molecules in an asymmetric unit were clearly seen in a 3.9 A electron density map. The main chains of three molecules were traced at 2.5 A resolution. The structure of the remaining one molecule, however, remains unknown because of the poor electron density of the corresponding region. The three main chain folds exhibit the same topology as that in Spirulina platensis. The structural similarity between A. sacrum and S. platensis ferredoxins, whose amino acid sequences are different from each other by about 30%, strongly suggests that all plant-type ferredoxins have the same main chain fold.

摘要

对蓝绿藻聚球藻属的一种[2Fe-2S]铁氧化还原蛋白I进行了分辨率为2.5埃的晶体结构分析。通过单同晶置换法结合铀衍生物的反常色散效应确定了每个反射的相角。在3.9埃的电子密度图中可以清楚地看到一个不对称单元中的四个分子。以2.5埃的分辨率追踪了三个分子的主链。然而,由于相应区域电子密度较差,其余一个分子的结构仍然未知。这三个主链折叠呈现出与钝顶螺旋藻相同的拓扑结构。聚球藻属和钝顶螺旋藻铁氧化还原蛋白之间的结构相似性,其氨基酸序列彼此相差约30%,强烈表明所有植物型铁氧化还原蛋白具有相同的主链折叠。

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