3A1S

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

Summary for 3A1S

• Entry DOI: 10.2210/pdb3a1s/pdb
• Related: 3AIT 3AIU 3AIV 3AIW
• Descriptor: Iron(II) transport protein B, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: feob, iron transporter, small gtpase, g protein, gdi, transport protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 60220.17

Authors

Hattori, M.,Ishitani, R.,Nureki, O. (deposition date: 2009-04-22, release date: 2009-09-22, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)