1EW4

CRYSTAL STRUCTURE OF ESCHERICHIA COLI CYAY PROTEIN REVEALS A NOVEL FOLD FOR THE FRATAXIN FAMILY

1EW4 の概要

• エントリーDOI: 10.2210/pdb1ew4/pdb
• 分子名称: CYAY PROTEIN (2 entities in total)
• 機能のキーワード: friedreich ataxia, frataxin family, cyay, iron homeostasis, unknown function
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12242.36

構造登録者

Suh, S.W.,Cho, S.,Lee, M.G.,Yang, J.K.,Lee, J.Y.,Song, H.K. (登録日: 2000-04-22, 公開日: 2000-08-09, 最終更新日: 2024-02-07)

主引用文献

Cho, S.J.,Lee, M.G.,Yang, J.K.,Lee, J.Y.,Song, H.K.,Suh, S.W.
Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family.
Proc.Natl.Acad.Sci.USA, 97:8932-8937, 2000

PubMed Abstract: Friedreich ataxia is an autosomal recessive neurodegenerative disease caused by defects in the FRDA gene, which encodes a mitochondrial protein called frataxin. Frataxin is evolutionarily conserved, with homologs identified in mammals, worms, yeast, and bacteria. The CyaY proteins of gamma-purple bacteria are believed to be closely related to the ancestor of frataxin. In this study, we have determined the crystal structure of the CyaY protein from Escherichia coli at 1.4-A resolution. It reveals a protein fold consisting of a six-stranded antiparallel beta-sheet flanked on one side by two alpha-helices. This fold is likely to be shared by all members of the conserved frataxin family. This study also provides a framework for the interpretation of disease-associated mutations in frataxin and for understanding the possible functions of this protein family.

PubMed: 10908679
DOI: 10.1073/pnas.160270897

実験手法

X-RAY DIFFRACTION (1.4 Å)