1S8J

Nitrate-bound D85S mutant of bacteriorhodopsin

1S8J の概要

• エントリーDOI: 10.2210/pdb1s8j/pdb
• 関連するPDBエントリー: 1MGY 1S8L
• 分子名称: Bacteriorhodopsin precursor, NITRATE ION, RETINAL, ... (5 entities in total)
• 機能のキーワード: bacteriorhodopsin, anion, pump, membrane protein
• 由来する生物種: Halobacterium sp.
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P02945
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31721.84

構造登録者

Facciotti, M.T.,Cheung, V.S.,Lunde, C.S.,Rouhani, S.,Baliga, N.S.,Glaeser, R.M. (登録日: 2004-02-02, 公開日: 2004-06-08, 最終更新日: 2023-08-23)

主引用文献

Facciotti, M.T.,Cheung, V.S.,Lunde, C.S.,Rouhani, S.,Baliga, N.S.,Glaeser, R.M.
Specificity of anion binding in the substrate pocket of bacteriorhodopsin.
Biochemistry, 43:4934-4943, 2004

PubMed Abstract: The structure of the D85S mutant of bacteriorhodopsin with a nitrate anion bound in the Schiff base binding site and the structure of the anion-free protein have been obtained in the same crystal form. Together with the previously solved structures of this anion pump, in both the anion-free state and bromide-bound state, these new structures provide insight into how this mutant of bacteriorhodopsin is able to bind a variety of different anions in the same binding pocket. The structural analysis reveals that the main structural change that accommodates different anions is the repositioning of the polar side chain of S85. On the basis of these X-ray crystal structures, the prediction is then made that the D85S/D212N double mutant might bind similar anions and do so over a broader pH range than does the single mutant. Experimental comparison of the dissociation constants, K(d), for a variety of anions confirms this prediction and demonstrates, in addition, that the binding affinity is dramatically improved by the D212N substitution.

PubMed: 15109251
DOI: 10.1021/bi035757s

実験手法

X-RAY DIFFRACTION (2.3 Å)