1OE2

Atomic Resolution Structure of D92E Mutant of Alcaligenes xylosoxidans Nitrite Reductase

1OE2 の概要

• エントリーDOI: 10.2210/pdb1oe2/pdb
• 関連するPDBエントリー: 1BQ5 1GS6 1GS7 1GS8 1HAU 1HAW 1NDT 1OE1
• 分子名称: DISSIMILATORY COPPER-CONTAINING NITRITE REDUCTASE, COPPER (II) ION, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: reductase, nitrite reductase, copper protein
• 由来する生物種: ALCALIGENES XYLOSOXIDANS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36888.84

構造登録者

Ellis, M.J.,Dodd, F.E.,Sawers, G.,Eady, R.R.,Hasnain, S.S. (登録日: 2003-03-18, 公開日: 2003-04-17, 最終更新日: 2024-11-20)

主引用文献

Ellis, M.J.,Dodd, F.E.,Sawers, G.,Eady, R.R.,Hasnain, S.S.
Atomic Resolution Structures of Native Copper Nitrite Reductase from Alcaligenes Xylosoxidans and the Active Site Mutant Asp92Glu
J.Mol.Biol., 328:429-, 2003

PubMed Abstract: We provide the first atomic resolution (<1.20 A) structure of a copper protein, nitrite reductase, and of a mutant of the catalytically important Asp92 residue (D92E). The atomic resolution where carbon-carbon bonds of the peptide become clearly resolved, remains a key goal of structural analysis. Despite much effort and technological progress, still very few structures are known at such resolution. For example, in the Protein Data Bank (PDB) there are some 200 structures of copper proteins but the highest resolution structure is that of amicyanin, a small (12 kDa) protein, which has been resolved to 1.30 A. Here, we present the structures of wild-type copper nitrite reductase (wtNiR) from Alcaligenes xylosoxidans (36.5 kDa monomer), the "half-apo" recombinant native protein and the D92E mutant at 1.04, 1.15 and 1.12A resolutions, respectively. These structures provide the basis from which to build a detailed mechanism of this important enzyme.

PubMed: 12691751
DOI: 10.1016/S0022-2836(03)00308-5

実験手法

X-RAY DIFFRACTION (1.12 Å)