2WJH

Structure and function of the FeoB G-domain from Methanococcus jannaschii

2WJH の概要

• エントリーDOI: 10.2210/pdb2wjh/pdb
• 関連するPDBエントリー: 2WJG 2WJI 2WJJ
• 分子名称: FERROUS IRON TRANSPORT PROTEIN B HOMOLOG, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: metal transport, membrane g-proteins, ferrous iron transport, cell membrane, ion transport, transmembrane, nucleotide binding motifs, iron, gnbps, membrane, transport, gtp-binding, iron transport, nucleotide-binding
• 由来する生物種: METHANOCALDOCOCCUS JANNASCHII
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37195.74

構造登録者

Koester, S.,Wehner, M.,Herrmann, C.,Kuehlbrandt, W.,Yildiz, O. (登録日: 2009-05-26, 公開日: 2009-07-28, 最終更新日: 2023-12-13)

主引用文献

Koester, S.,Wehner, M.,Herrmann, C.,Kuehlbrandt, W.,Yildiz, O.
Structure and Function of the Feob G-Domain from Methanococcus Jannaschii
J.Mol.Biol., 392:405-, 2009

PubMed Abstract: FeoB in bacteria and archaea is involved in the uptake of ferrous iron (Fe(2+)), an important cofactor in biological electron transfer and catalysis. Unlike any other known prokaryotic membrane protein, FeoB contains a GTP-binding domain at its N-terminus. We determined high-resolution X-ray structures of the FeoB G-domain from Methanococcus jannaschii with and without bound GDP or Mg(2+)-GppNHp. The G-domain forms the same dimer in all three structures, with the nucleotide-binding pockets at the dimer interface, as in the ATP-binding domain of ABC transporters. The G-domain follows the typical fold of nucleotide-binding proteins, with a beta-strand inserted in switch I that becomes partially disordered upon GTP binding. Switch II does not contact the nucleotide directly and does not change its conformation in response to the bound nucleotide. Release of the nucleotide causes a rearrangement of loop L6, which we identified as the G5 region of FeoB. Together with the C-terminal helix, this loop may transmit the information about the nucleotide-bound state from the G-domain to the transmembrane region of FeoB.

PubMed: 19615379
DOI: 10.1016/J.JMB.2009.07.020

実験手法

X-RAY DIFFRACTION (2.1 Å)