1AZN

CRYSTAL STRUCTURE OF THE AZURIN MUTANT PHE114ALA FROM PSEUDOMONAS AERUGINOSA AT 2.6 ANGSTROMS RESOLUTION

1AZN の概要

• エントリーDOI: 10.2210/pdb1azn/pdb
• 分子名称: AZURIN, COPPER (II) ION (3 entities in total)
• 機能のキーワード: electron transport(copper binding)
• 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: 55796.99

構造登録者

Tsai, L.-C.,Sjolin, L.,Langer, V.,Pascher, T.,Nar, H. (登録日: 1994-05-27, 公開日: 1994-10-15, 最終更新日: 2024-02-07)

主引用文献

Tsai, L.C.,Sjolin, L.,Langer, V.,Pascher, T.,Nar, H.
Structure of the azurin mutant Phe114Ala from Pseudomonas aeruginosa at 2.6 A resolution.
Acta Crystallogr.,Sect.D, 51:168-176, 1995

PubMed Abstract: The crystal structure of azurin mutant Phe114Ala from Pseudomonas aeruginosa has been solved by molecular replacement. The final crystallographic R value is 0.185 for 9832 reflections to a resolution of 2.6 A. The root-mean-square deviation for main-chain atom positions is 0.020 A between the four independent monomers in the asymmetric unit. The mutant Ala114 crystallized from PEG 4000 in a new crystal form and the crystals are monoclinic, P2(1), a= 51.0, b = 83.6, c= 66.4 A and beta = 110.5 degrees. The four molecules in the asymmetric unit are packed as a dimer of dimers and are related by an approximate twofold axis. The dimer packing and the dimer contact region are very similar to that of the Alcaligenes denitrificans azurin dimer. The mutation was performed at residue Phe114, which exhibits a pi-electron overlap with the copper ligand His117, to investigate its suggested role in the electron self-exchange reaction. Removal of steric constrains from the phenylalanine side chain created a somewhat different geometry around the copper site with an increased mobility of His117 resulting in an enlarged Cu-N length which may be responsible for the slight differences obtained in the spectral properties of the mutant versus the wild-type protein.

PubMed: 15299318
DOI: 10.1107/S0907444994005627

実験手法

X-RAY DIFFRACTION (2.6 Å)