2D2A

Crystal Structure of Escherichia coli SufA Involved in Biosynthesis of Iron-sulfur Clusters

2D2A の概要

• エントリーDOI: 10.2210/pdb2d2a/pdb
• 分子名称: SufA protein (2 entities in total)
• 機能のキーワード: iron-sulfur cluster, iron, suf, sufa, isca, yadr, 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: 32153.92

構造登録者

Wada, K.,Hasegawa, Y.,Gong, Z.,Minami, Y.,Fukuyama, K.,Takahashi, Y. (登録日: 2005-09-05, 公開日: 2005-12-13, 最終更新日: 2023-10-25)

主引用文献

Wada, K.,Hasegawa, Y.,Gong, Z.,Minami, Y.,Fukuyama, K.,Takahashi, Y.
Crystal structure of Escherichia coli SufA involved in biosynthesis of iron-sulfur clusters: Implications for a functional dimer
Febs Lett., 579:6543-6548, 2005

PubMed Abstract: IscA and SufA are paralogous proteins that play crucial roles in the biosynthesis of Fe-S clusters, perhaps through a mechanism involving transient Fe-S cluster formation. We have determined the crystal structure of E. coli SufA at 2.7A resolution. SufA exists as a homodimer, in contrast to the tetrameric organization of IscA. Furthermore, a C-terminal segment containing two essential cysteine residues (Cys-Gly-Cys), which is disordered in the IscA structure, is clearly visible in one molecule (the alpha1 subunit) of the SufA homodimer. Although this segment is disordered in the other molecule (the alpha2 subunit), computer modeling of this segment based on the well-defined conformation of alpha1 subunit suggests that the four cysteine residues (Cys114 and Cys116 in each subunit) in the Cys-Gly-Cys motif are positioned in close proximity at the dimer interface. The arrangement of these cysteines together with the nearby Glu118 in SufA dimer may allow coordination of an Fe-S cluster and/or an Fe atom.

PubMed: 16298366
DOI: 10.1016/j.febslet.2005.10.046

実験手法

X-RAY DIFFRACTION (2.7 Å)