3V5Y

Structure of FBXL5 hemerythrin domain, P2(1) cell

3V5Y の概要

• エントリーDOI: 10.2210/pdb3v5y/pdb
• 関連するPDBエントリー: 3V5X 3V5Z
• 分子名称: F-box/LRR-repeat protein 5, MU-OXO-DIIRON (3 entities in total)
• 機能のキーワード: hemerythrin, alpha helical bundle, e3 ubiquitin ligase complex, gene regulation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, perinuclear region : Q9UKA1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 77943.30

構造登録者

Tomchick, D.R.,Bruick, R.K.,Thompson, J.W.,Brautigam, C.A. (登録日: 2011-12-17, 公開日: 2012-01-25, 最終更新日: 2023-09-13)

主引用文献

Thompson, J.W.,Salahudeen, A.A.,Chollangi, S.,Ruiz, J.C.,Brautigam, C.A.,Makris, T.M.,Lipscomb, J.D.,Tomchick, D.R.,Bruick, R.K.
Structural and Molecular Characterization of Iron-sensing Hemerythrin-like Domain within F-box and Leucine-rich Repeat Protein 5 (FBXL5).
J.Biol.Chem., 287:7357-7365, 2012

PubMed Abstract: Mammalian cells maintain iron homeostasis by sensing changes in bioavailable iron levels and promoting adaptive responses. FBXL5 is a subunit of an E3 ubiquitin ligase complex that mediates the stability of iron regulatory protein 2, an important posttranscriptional regulator of several genes involved in iron metabolism. The stability of FBXL5 is regulated in an iron- and oxygen-responsive manner, contingent upon the presence of its N-terminal domain. Here we present the atomic structure of the FBXL5 N terminus, a hemerythrin-like α-helical bundle fold not previously observed in mammalian proteins. The core of this domain employs an unusual assortment of amino acids necessary for the assembly and sensing properties of its diiron center. These regulatory features govern the accessibility of a mapped sequence required for proteasomal degradation of FBXL5. Detailed molecular and structural characterization of the ligand-responsive hemerythrin domain provides insights into the mechanisms by which FBXL5 serves as a unique mammalian metabolic sensor.

PubMed: 22253436
DOI: 10.1074/jbc.M111.308684

実験手法

X-RAY DIFFRACTION (2.1 Å)