Revelation of endogenously bound Fe2+ ions in the crystal structure of ferritin from Escherichia coli

被引：3

作者：

Thiruselvam, Viswanathan ^{[1
]}

Sivaraman, Padavattan ^{[2
]}

Kumarevel, Thirumananseri ^{[2
,3
]}

Ponnuswamy, Mondikalipudur Nanjappagounder ^{[1
]}

机构：

[1] Univ Madras, Ctr Adv Study Crystallog & Biophys, Madras 600025, Tamil Nadu, India

[2] RIKEN SPring 8 Ctr, Harima Inst, Sayo, Hyogo 6795148, Japan

[3] RIKEN, RIKEN Yokohama Inst, Struct Biol Lab, Yokohama, Kanagawa 2300045, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2014年 / 453卷 / 03期

关键词：

Ferritin; Iron regulation; Binuclear iron site; HUMAN H-FERRITIN; APOFERRITIN; RESOLUTION; PROTEIN;

D O I：

10.1016/j.bbrc.2014.10.007

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ferritin is an iron regulatory protein. It is responsible for storage and detoxification of excess iron thereby it regulates iron level in the body. Here we report the crystal structure of ferritin with two endogenously expressed Fe atoms binding in both the sites. The protein was purified and characterized by MALDI-TOF and N-terminal amino acid sequencing. The crystal belongs to 14 space group and it diffracted up to 2.5 angstrom. The structural analysis suggested that it crystallizes as hexamer and confirmed that it happened to be the first report of endogenously expressed Fe ions incorporated in both the A and B sites, situated in between the helices. (C) 2014 Elsevier Inc. All rights reserved.

引用

页码：636 / 641

页数：6

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