1ILS

X-RAY CRYSTAL STRUCTURE THE TWO SITE-SPECIFIC MUTANTS ILE7SER AND PHE110SER OF AZURIN FROM PSEUDOMONAS AERUGINOSA

1ILS の概要

• エントリーDOI: 10.2210/pdb1ils/pdb
• 分子名称: AZURIN, COPPER (II) ION, NITRATE ION, ... (4 entities in total)
• 機能のキーワード: electron transfer protein, metalloprotein
• 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: 56059.07

構造登録者

Hammann, C.,Nar, H.,Huber, R.,Messerschmidt, A. (登録日: 1995-10-12, 公開日: 1996-03-08, 最終更新日: 2024-10-23)

主引用文献

Hammann, C.,Messerschmidt, A.,Huber, R.,Nar, H.,Gilardi, G.,Canters, G.W.
X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa.
J.Mol.Biol., 255:362-366, 1996

PubMed Abstract: The blue copper protein azurin from Pseudomonas aeruginosa contains a single Trp residue that is believed to be involved in the inducible intramolecular electron transfer from a disulphide group to the copper centre. This residue shows in fluorescence spectra the highest energy emission of tryptophan-containing compounds at room temperature, which is explained by its rigid and highly hydrophobic environment. In order to investigate the role of the Trp residue in electron transfer and the influence of its environment, two mutations (17S and F110S) were introduced that were thought to increase the polarity and the mobility in its environment. The crystal structures of these mutants were solved at 2.2 A and 2.3 A resolution, respectively. These provide a structural basis for the changes observed in fluorescence spectra compared with the wild-type protein. We conclude from our results that these changes are not caused by a change in the dynamics of the Trp residue itself, but exclusively by an increased effective dielectric constant of the microenvironment of Trp48 and by changes in mobility of the mutated residues.

PubMed: 8568881
DOI: 10.1006/jmbi.1996.0029

実験手法

X-RAY DIFFRACTION (2.2 Å)