2TSB

AZURIN MUTANT M121A-AZIDE

「1TSB」から置き換えられました

2TSB の概要

• エントリーDOI: 10.2210/pdb2tsb/pdb
• 分子名称: AZURIN AZIDE, AZIDE ION, COPPER (II) ION, ... (4 entities in total)
• 機能のキーワード: electron transport
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Periplasm: P00282
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56028.99

構造登録者

Tsai, L.-C.,Bonander, N.,Harata, K.,Karlsson, B.G.,Vanngard, T.,Langer, V.,Sjolin, L. (登録日: 1996-05-10, 公開日: 1996-11-08, 最終更新日: 2024-10-16)

主引用文献

Tsai, L.C.,Bonander, N.,Harata, K.,Karlsson, G.,Vanngard, T.,Langer, V.,Sjolin, L.
Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative: crystal structures and spectral properties.
Acta Crystallogr.,Sect.D, 52:950-958, 1996

PubMed Abstract: The crystal structures of the azurin mutant Met121Ala and its azide derivative Met121Ala-azide from Pseudomonas aeruginosa have been determined. The final crystallographic R values are 21.3 and 19.4% for the two structures, respectively. In the Met121Ala mutant, the distance between the copper ion and His117 increases by 0.34 A compared with the wild-type structure. The removal of the methionine in the apical position induces a shortening of the distance from the copper ion to the carbonyl O atom of Gly45 from 2.97 to 2.74 A. In the Met121Ala-azide structure, the azide anion occupies the cavity created by replacing the Met121 side chain with the smaller methyl group of Ala. The azide anion binds with a terminal N atom to the copper ion at a distance of about 2.04 A. In addition, the copper ion has moved out of the trigonal plane by about 0.26 A towards the azide anion. Thus, the copper site in this structure has a distorted tetrahedral arrangement. The spectroscopic characteristics show, in addition, that the copper sites in the two structures are distinctively different. The Met121Ala mutant still maintains the properties of an ordinary type 1 copper site while the Met121Ala-azide derivative has an absorption maximum at about 409 nm and the copper hyperfine coupling has increased to a value intermediate between those of type 2 copper and the wild-type azurin.

PubMed: 15299604
DOI: 10.1107/S0907444996004982

実験手法

X-RAY DIFFRACTION (2.3 Å)