6FA0

Lysozyme crystallized in presence of 100 mM ammonium sulphate at pH 4.5

Summary for 6FA0

• Entry DOI: 10.2210/pdb6fa0/pdb
• Descriptor: Lysozyme C, CHLORIDE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: Gallus gallus (Chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14192.32

Authors

Camara-Artigas, A. (deposition date: 2017-12-15, release date: 2018-05-09, Last modification date: 2024-11-13)

Primary citation

Plaza-Garrido, M.,Salinas-Garcia, M.C.,Camara-Artigas, A.
Orthorhombic lysozyme crystallization at acidic pH values driven by phosphate binding.
Acta Crystallogr D Struct Biol, 74:480-489, 2018

PubMed Abstract: The structure of orthorhombic lysozyme has been obtained at 298 K and pH 4.5 using sodium chloride as the precipitant and in the presence of sodium phosphate at a concentration as low as 5 mM. Crystals belonging to space group P222 (unit-cell parameters a = 30, b = 56, c = 73 Å, α = β = γ = 90.00°) diffracted to a resolution higher than 1 Å, and the high quality of these crystals permitted the identification of a phosphate ion bound to Arg14 and His15. The binding of this ion produces long-range conformational changes affecting the loop containing Ser60-Asn74. The negatively charged phosphate ion shields the electrostatic repulsion of the positively charged arginine and histidine residues, resulting in higher stability of the phosphate-bound lysozyme. Additionally, a low-humidity orthorhombic variant was obtained at pH 4.5, and comparison with those previously obtained at pH 6.5 and 9.5 shows a 1.5 Å displacement of the fifth α-helix towards the active-site cavity, which might be relevant to protein function. Since lysozyme is broadly used as a model protein in studies related to protein crystallization and amyloid formation, these results indicate that the interaction of some anions must be considered when analysing experiments performed at acidic pH values.

PubMed: 29717719
DOI: 10.1107/S205979831800517X

Experimental method

X-RAY DIFFRACTION (1.3 Å)