3A1T

Crystal structue of the cytosolic domain of T. maritima FeoB iron iransporter in GDP form II

3A1T の概要

• エントリーDOI: 10.2210/pdb3a1t/pdb
• 関連するPDBエントリー: 3AIS 3AIU 3AIV 3AIW
• 分子名称: Iron(II) transport protein B, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: feob, iron transpoter, small gtpase, g protein, gdi, transport protein
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29674.05

構造登録者

Hattori, M.,Ishitani, R.,Nureki, O. (登録日: 2009-04-22, 公開日: 2009-09-22, 最終更新日: 2023-11-01)

主引用文献

Hattori, M.,Jin, Y.,Nishimasu, H.,Tanaka, Y.,Mochizuki, M.,Uchiumi, T.,Ishitani, R.,Ito, K.,Nureki, O.
Structural basis of novel interactions between the small-GTPase and GDI-like domains in prokaryotic FeoB iron transporter
Structure, 17:1345-1355, 2009

PubMed Abstract: The FeoB family proteins are widely distributed prokaryotic membrane proteins involved in Fe(2+) uptake. FeoB consists of N-terminal cytosolic and C-terminal transmembrane domains. The N-terminal region of the cytosolic domain is homologous to small GTPase (G) proteins and is considered to regulate Fe(2+) uptake. The spacer region connecting the G and TM domains reportedly functions as a GDP dissociation inhibitor (GDI)-like domain that stabilizes the GDP-binding state. However, the function of the G and GDI-like domains in iron uptake remains unclear. Here, we report the structural and functional analyses of the FeoB cytosolic domain from Thermotoga maritima. The structure-based mutational analysis indicated that the interaction between the G and GDI-like domains is important for both the GDI and Fe(2+) uptake activities. On the basis of these results, we propose a regulatory mechanism of Fe(2+) uptake.

PubMed: 19733088
DOI: 10.1016/j.str.2009.08.007

実験手法

X-RAY DIFFRACTION (1.8 Å)