2BBH

X-ray structure of T.maritima CorA soluble domain

2BBH の概要

• エントリーDOI: 10.2210/pdb2bbh/pdb
• 関連するPDBエントリー: 2BBJ
• 分子名称: divalent cation transport-related protein, DECYL-BETA-D-MALTOPYRANOSIDE, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: transporter, mg, membrane, structural genomics, structural genomics consortium, sgc, metal transport-membrane protein complex, metal transport/membrane protein
• 由来する生物種: Thermotoga maritima
• 細胞内の位置: Cell inner membrane ; Multi-pass membrane protein : Q9WZ31
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34142.63

構造登録者

Lunin, V.V.,Dobrovetsky, E.,Khutoreskaya, G.,Bochkarev, A.,Maguire, M.E.,Edwards, A.M.,Koth, C.M.,Structural Genomics Consortium (SGC) (登録日: 2005-10-17, 公開日: 2005-12-13, 最終更新日: 2024-11-13)

主引用文献

Lunin, V.V.,Dobrovetsky, E.,Khutoreskaya, G.,Zhang, R.,Joachimiak, A.,Doyle, D.A.,Bochkarev, A.,Maguire, M.E.,Edwards, A.M.,Koth, C.M.
Crystal structure of the CorA Mg2+ transporter.
Nature, 440:833-837, 2006

PubMed Abstract: The magnesium ion, Mg2+, is essential for myriad biochemical processes and remains the only major biological ion whose transport mechanisms remain unknown. The CorA family of magnesium transporters is the primary Mg2+ uptake system of most prokaryotes and a functional homologue of the eukaryotic mitochondrial magnesium transporter. Here we determine crystal structures of the full-length Thermotoga maritima CorA in an apparent closed state and its isolated cytoplasmic domain at 3.9 A and 1.85 A resolution, respectively. The transporter is a funnel-shaped homopentamer with two transmembrane helices per monomer. The channel is formed by an inner group of five helices and putatively gated by bulky hydrophobic residues. The large cytoplasmic domain forms a funnel whose wide mouth points into the cell and whose walls are formed by five long helices that are extensions of the transmembrane helices. The cytoplasmic neck of the pore is surrounded, on the outside of the funnel, by a ring of highly conserved positively charged residues. Two negatively charged helices in the cytoplasmic domain extend back towards the membrane on the outside of the funnel and abut the ring of positive charge. An apparent Mg2+ ion was bound between monomers at a conserved site in the cytoplasmic domain, suggesting a mechanism to link gating of the pore to the intracellular concentration of Mg2+.

PubMed: 16598263
DOI: 10.1038/nature04642

実験手法

X-RAY DIFFRACTION (1.85 Å)