6f1m | pdb_00006f1m

Lysozyme crystallized in presence of 100 mM sodium phosphate at pH 4.5: low-humidity form

spinqualitylabelsall models 6f1m, resolution 1.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6f1m is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Lysozyme, with EC number 3.2.1.17 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus. Publication Abstract from PubMed 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 P212121 (unit-cell parameters a = 30, b = 56, c = 73 A, alpha = beta = gamma = 90.00 degrees ) diffracted to a resolution higher than 1 A, 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 A displacement of the fifth alpha-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. Orthorhombic lysozyme crystallization at acidic pH values driven by phosphate binding.,Plaza-Garrido M, Salinas-Garcia MC, Camara-Artigas A Acta Crystallogr D Struct Biol. 2018 May 1;74(Pt 5):480-489. doi:, 10.1107/S205979831800517X. Epub 2018 Apr 27. PMID:29717719 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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