1NZR

CRYSTAL STRUCTURE OF THE AZURIN MUTANT NICKEL-TRP48MET FROM PSEUDOMONAS AERUGINOSA AT 2.2 ANGSTROMS RESOLUTION

Summary for 1NZR

• Entry DOI: 10.2210/pdb1nzr/pdb
• Descriptor: AZURIN, NICKEL (II) ION, NITRATE ION, ... (4 entities in total)
• Functional Keywords: electron transport (copper)
• Biological source: Pseudomonas aeruginosa
• Cellular location: Periplasm: P00282
• Total number of polymer chains: 4
• Total formula weight: 55923.91

Authors

Tsai, L.-C.,Sjolin, L.,Langer, V.,Bonander, N.,Karlsson, B.G.,Vanngard, T.,Hammann, C.,Nar, H. (deposition date: 1994-12-09, release date: 1995-02-27, Last modification date: 2024-10-16)

Primary citation

Tsai, L.C.,Sjolin, L.,Langer, V.,Bonander, N.,Karlsson, B.G.,Vanngard, T.,Hammann, C.,Nar, H.
Structure of the azurin mutant nickel-Trp48Met from Pseudomonas aeruginosa at 2.2 A resolution.
Acta Crystallogr.,Sect.D, 51:711-717, 1995

PubMed Abstract: The structure of the azurin mutant nickel-Trp48Met from Pseudomonas aeruginosa has been determined by difference Fourier synthesis using phases from the wild-type azurin model. The final crystallographic R value is 0.170 for 17 394 reflections to a resolution of 2.2 A. The mutant crystallized in the orthorhombic space group P2(1)2(1)2(1), a = 57.4, b = 80.4, c = 110.3 A. The four molecules in the asymmetric unit are packed as a dimer of dimers. The nickel metal site of this mutant structure is similar to the zinc metal site in the azurin Asp47 mutant. The site-specific mutation was performed at residue Trp48, which is located in the center of the protein in a highly hydrophobic environment, to investigate its suggested role in the long-range electron-transfer pathway between the disulfide bond on one side of the protein to the Cu centre. The structure around the mutation site Met48 showed no significant change compared with the wild-type structure.

PubMed: 15299800
DOI: 10.1107/S0907444995001041

Experimental method

X-RAY DIFFRACTION (2.2 Å)