3a1t | pdb_00003a1t

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

spinqualitylabelsall models 3a1t, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3a1t is a 1 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP Related: 3ais, 3aiu, 3aiv, 3aiw Gene: TM0051 (ATCC 43589) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis of novel interactions between the small-GTPase and GDI-like domains in prokaryotic FeoB iron transporter.,Hattori M, Jin Y, Nishimasu H, Tanaka Y, Mochizuki M, Uchiumi T, Ishitani R, Ito K, Nureki O Structure. 2009 Oct 14;17(10):1345-55. Epub 2009 Sep 3. PMID:19733088 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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