2BZT

NMR structure of the bacterial protein YFHJ from E. coli

2BZT の概要

• エントリーDOI: 10.2210/pdb2bzt/pdb
• NMR情報: BMRB: 6776
• 分子名称: PROTEIN ISCX (1 entity in total)
• 機能のキーワード: iron binding protein, iron sulphur clusters, isc operon, isc proteins
• 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: 7737.53

構造登録者

Pastore, C.,Kelly, G.,Adinolfi, S.,Mc Cormick, J.E.,Pastore, A. (登録日: 2005-08-22, 公開日: 2006-12-06, 最終更新日: 2024-05-15)

主引用文献

Pastore, C.,Adinolfi, S.,Huynen, M.A.,Rybin, V.,Martin, S.,Mayer, M.,Bukau, B.,Pastore, A.
YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein?
Structure, 14:857-867, 2006

PubMed Abstract: The yfhJ gene is part of the isc operon, which encodes the machinery devoted to assemble iron-sulfur clusters in prokaryotes. Its transcript is a small acidic protein that binds the desulfurase IscS, which is essential in iron-specific metabolic pathways. To understand its cellular role, we have characterized the structure of YfhJ in solution and its interactions with potential cellular partners. It contains a modified winged helix motif, usually present in DNA binding proteins, and is able to bind iron cations. The IscS interaction surface is the same as that involved in iron binding. This observation and the pattern of conservation through species strongly suggest that YfhJ is a molecular adaptor that is able to modulate the function of IscS in iron-sulfur cluster formation. The remarkable similarity between the in vitro behavior of YfhJ and that of the protein frataxin also suggests new hypotheses regarding the functional role of both proteins.

PubMed: 16698547
DOI: 10.1016/j.str.2006.02.010

実験手法

SOLUTION NMR