1hf4
From Proteopedia
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STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME CRYSTALS
Overview
Understanding direct salt effects on protein crystal polymorphism is, addressed by comparing different crystal forms (triclinic, monoclinic, tetragonal and orthorhombic) for hen, turkey, bob white quail and human, lysozymes. Four new structures of hen egg-white lysozyme are reported:, crystals grown in the presence of NapTS diffracted to 1.85 A, of NaI to, 1.6 A, of NaNO(3) to 1.45 A and of KSCN to 1.63 A. These new structures, are compared with previously published structures in order to draw a, mapping of the surface of different lysozymes interacting with monovalent, anions, such as nitrate, chloride, iodide, bromide and thiocyanate. An, analysis of the structural sites of these anions in the various lysozyme, structures is presented. This study shows common anion sites whatever the, crystal form and the chemical nature of anions, while others seem specific, to a given geometry and a particular charge environment induced by the, crystal packing.
About this Structure
1HF4 is a Single protein structure of sequence from Gallus gallus with and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Known structural/functional Sites: , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Structural effects of monovalent anions on polymorphic lysozyme crystals., Vaney MC, Broutin I, Retailleau P, Douangamath A, Lafont S, Hamiaux C, Prange T, Ducruix A, Ries-Kautt M, Acta Crystallogr D Biol Crystallogr. 2001 Jul;57(Pt 7):929-40. Epub 2001, Jun 21. PMID:11418760
Page seeded by OCA on Sun Feb 3 09:48:57 2008
Categories: Gallus gallus | Lysozyme | Single protein | Broutin, I. | Ducruix, A. | Ries-Kautt, M. | Vaney, M.C. | NA | NO3 | Hydrolase | Hydrolase (o-glycosyl)
