Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA

被引：229

作者：

Walden, William E.

Selezneva, Anna I.

Dupuy, Jerome

Volbeda, Anne

Fontecilla-Camps, Juan C.

Theil, Elizabeth C.

Volz, Karl ^{[1
]}

机构：

[1] Univ Illinois, Dept Microbiol & Immunol, Chicago, IL 60612 USA

[2] Univ Grenoble 1, Inst Biol Struct Jean Pierre Horowitz, IBS, Lab Cristallog & Cristallog Prot, F-38207 Grenoble, France

[3] Univ Grenoble 1, CEA, F-38207 Grenoble, France

[4] Univ Grenoble 1, CNRS, F-38207 Grenoble, France

[5] Childrens Hosp, Oakland Res Inst, Oakland, CA 94609 USA

[6] Univ Calif Berkeley, Dept Nutr Sci & Mol Toxicol, Berkeley, CA 94720 USA

来源：

SCIENCE | 2006年 / 314卷 / 5807期

关键词：

D O I：

10.1126/science.1133116

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Iron regulatory protein 1 (IRP1) binds iron-responsive elements (IREs) in messenger RNAs (mRNAs), to repress translation or degradation, or binds an iron-sulfur cluster, to become a cytosolic aconitase enzyme. The 2.8 angstrom resolution crystal structure of the IRP1: ferritin H IRE complex shows an open protein conformation compared with that of cytosolic aconitase. The extended, L-shaped IRP1 molecule embraces the IRE stem-loop through interactions at two sites separated by similar to 30 angstroms, each involving about a dozen protein: RNA bonds. Extensive conformational changes related to binding the IRE or an iron-sulfur cluster explain the alternate functions of IRP1 as an mRNA regulator or enzyme.

引用

页码：1903 / 1908

页数：6

共 37 条

[1] Structure and dynamics of the iron responsive element RNA: Implications for binding of the RNA by iron regulatory binding proteins [J].