1R95

Crystal Structure of IscA (native)

1R95 の概要

• エントリーDOI: 10.2210/pdb1r95/pdb
• 関連するPDBエントリー: 1R94
• 分子名称: Protein yfhF (2 entities in total)
• 機能のキーワード: tetrameric, beta barrel, iron-sulfur cluster protein, pseudo-asymmetric motifs, metal transport
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25686.88

構造登録者

Bilder, P.W.,Ding, H.,Newcomer, M.E. (登録日: 2003-10-28, 公開日: 2003-12-23, 最終更新日: 2024-02-14)

主引用文献

Bilder, P.W.,Ding, H.,Newcomer, M.E.
Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold.
Biochemistry, 43:133-139, 2004

PubMed Abstract: IscA belongs to an ancient family of proteins responsible for iron-sulfur cluster assembly in essential metabolic pathways preserved throughout evolution. We report here the 2.3 A resolution crystal structure of Escherichia coli IscA, a novel fold in which mixed beta-sheets form a compact alpha-beta sandwich domain. In contrast to the highly mobile secondary structural elements within the bacterial Fe-S scaffold protein IscU, a protein which is thought to have a similar function, the great majority of the amino acids that are conserved in IscA homologues are located in elements that constitute a well-ordered fold. However, the 10-residue C-terminal tail segment that contains two invariant cysteines critical for the Fe-S-binding function of a cyanobacterial (Synechocystis PCC) IscA homologue is not ordered in our structure. In addition, the crystal packing reveals a helical assembly that is constructed from two possible tetrameric oligomers of IscA.

PubMed: 14705938

実験手法

X-RAY DIFFRACTION (2.65 Å)