Crystal Structure of the Ancient,Fe-S Scaffold IscA Reveals a Novel Protein Fold

Patrick W.Bilder; Huangen Ding; Marcia E.Newcomer

首页> 外文期刊>Biochemistry >Crystal Structure of the Ancient,Fe-S Scaffold IscA Reveals a Novel Protein Fold

【24h】

Crystal Structure of the Ancient,Fe-S Scaffold IscA Reveals a Novel Protein Fold

机译：古代Fe-S脚手架ISCA的水晶结构揭示了一种新的蛋白质折叠

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相似文献
相关主题

摘要

IscA belongs to an ancient family of proteins responsible form iron-sulfur cluster assembly in essential metabolic pathways preserved throughout evolution.We report here the 2.3 A resolution crystal structure of Escherichia coli IscA,a novel fold in which mixed beta-sheets form a compact alpha-beta sandwich domain.In contrast to the highly mobile secondary structural elements within the bacterial Fe-S scaffold protein IscU,a protein which is thought to have a similar function,the great majority of the amino acids that are conserved in IscA homologues are located in elements that constitute a well-ordered fold.However,the 10-residue C-terminal tail segment that contains two invariant cysteines critical for the Fe-S-binding function of a cyanobacterial (Synechocystis PCC) IscA homologue is not ordered in our structure.In addition,the crystal packing reveals a helical assembly that is constructed from two possible tetrameric oligomers of IscA.

机译：ISCA属于古代蛋白质蛋白质负责，在整个进化中保存的基本代谢途径中的古代蛋白质。在此报告的是2.3大肠杆菌ISCA的分辨率晶体结构，一种新型折叠，其中混合β-片形成紧凑型α- -beta sandwich domain.in与细菌Fe-s支架蛋白ISCU中的高度移动二级结构元素相比，被认为具有类似功能的蛋白质，在ISCA同源物中保守的大多数氨基酸在构成有序折叠的元件中。然而，在我们的结构中没有排序，含有两种含有两种不变性半胱氨酸的10-残基C末端尾段，其结构加法，晶体包装揭示了由ISCA的两种可能的四聚体低聚物构成的螺旋组件。

著录项

来源
《Biochemistry》 |2004年第1期|共7页
作者
Patrick W.Bilder; Huangen Ding; Marcia E.Newcomer;
展开▼
作者单位

Department of Biological Sciences Louisiana State University Baton Rouge Louisiana 70803;

Department of Biological Sciences Louisiana State University Baton Rouge Louisiana 70803;

Department of Biological Sciences Louisiana State University Baton Rouge Louisiana 70803;

展开▼
收录信息
原文格式 PDF
正文语种 eng
中图分类生物化学;
关键词

相似文献

外文文献
中文文献
专利

1. Crystal Structure of the Ancient,Fe-S Scaffold IscA Reveals a Novel Protein Fold [J] . Patrick W.Bilder, Huangen Ding, Marcia E.Newcomer Biochemistry . 2004,第1期

机译：古代Fe-S脚手架ISCA的水晶结构揭示了一种新的蛋白质折叠
2. Crystal structures of human secretory proteins ZG16p and ZG16b reveal a Jacalin-related beta-prism fold. [J] . Kanagawa M, Satoh T, Ikeda A, Biochemical and Biophysical Research Communications . 2011,第1期

机译：人类分泌蛋白ZG16p和ZG16b的晶体结构揭示了Jacalin相关的β棱镜折叠。
3. Crystal structures of human secretory proteins ZG16p and ZG16b reveal a Jacalin-related beta-prism fold. [J] . Kanagawa M, Satoh T, Ikeda A, Biochemical and Biophysical Research Communications . 2011,第1期

机译：人类分泌蛋白ZG16p和ZG16b的晶体结构揭示了Jacalin相关的β棱镜折叠。
4. Atomic Structure of Bordetella Bacteriophage Reveals a Jellyroll Fold in CementProtein and a Topologically Distinct HK97-like Fold in Major Capsid Protein [C] . Xing Zhang, Huatao Guo, Lei Jin, Microscopy Society of America Annual Meeting;Microanalysis Society Annual meeting;International Metallographic Society Annual meeting . 2012

机译：博德特氏菌噬菌体的原子结构揭示了水泥蛋白中的果冻折叠和主要衣壳蛋白中拓扑不同的HK97样折叠。
5. Structural studies of truncated human apolipoprotein A-I in solution and crystal identify the folding domain and reveal the assembly of discoidal HDL by dimerization [D] . Mei, Xiaohu 2011

机译：截短的人类载脂蛋白A-I在溶液和晶体中的结构研究确定了折叠域并通过二聚化揭示了盘状HDL的组装
6. Crystal structure of an Fe-S cluster-containing fumarate hydratase enzyme from Leishmania major reveals a unique protein fold [O] . Patricia R. Feliciano, Catherine L. Drennan, M. Cristina Nonato 2016

机译：利什曼原虫含有Fe-S簇的富马酸盐水合酶的晶体结构揭示了独特的蛋白质折叠
7. The Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase Reveals an Ancient Fold for an Ancient Enzyme [O] . Jian Payandeh, Masahiro Fujihashi, Wanda Gillon, 2006

机译：（S）-3-O-甘油基酰基甘油甘油合酶的晶体结构揭示了古代酶的古代折叠

Crystal Structure of the Ancient,Fe-S Scaffold IscA Reveals a Novel Protein Fold

摘要

著录项

相似文献

相关主题

期刊订阅