1D2E

CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP

1D2E の概要

• エントリーDOI: 10.2210/pdb1d2e/pdb
• 関連するPDBエントリー: 1EFC 1TUI
• 分子名称: ELONGATION FACTOR TU (EF-TU), MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: g-protein, beta-barrel, rna binding protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Mitochondrion: P49410
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 177035.57

構造登録者

Andersen, G.R.,Thirup, S.,Spremulli, L.L.,Nyborg, J. (登録日: 1999-09-23, 公開日: 1999-09-28, 最終更新日: 2024-02-07)

主引用文献

Andersen, G.R.,Thirup, S.,Spremulli, L.L.,Nyborg, J.
High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP.
J.Mol.Biol., 297:421-436, 2000

PubMed Abstract: The crystal structure of bovine mitochondrial elongation factor Tu (EF-Tu) in complex with GDP has been determined at a resolution of 1. 94 A. The structure is similar to that of EF-Tu:GDP from Escherichia coli and Thermus aquaticus, but the orientation of the GDP-binding domain 1 is changed relative to domains 2 and 3. Sixteen conserved water molecules common to EF-Tu and other G-proteins in the GDP-binding site are described. These water molecules create a network linking separated parts of the binding pocket. Mitochondrial EF-Tu binds nucleotides less tightly than prokaryotic EF-Tu possibly due to an increased mobility in regions close to the GDP-binding site. The C-terminal extension of mitochondrial EF-Tu has structural similarities with DNA recognising zinc fingers suggesting that the extension may be involved in recognition of RNA.

PubMed: 10715211
DOI: 10.1006/jmbi.2000.3564

実験手法

X-RAY DIFFRACTION (1.94 Å)