1hf4
From Proteopedia
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==Overview== | ==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, . | + | 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== | ==About this Structure== | ||
| - | 1HF4 is a | + | 1HF4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NA and NO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9 and BC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HF4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:00:07 2007'' |
Revision as of 12:54, 5 November 2007
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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 NA and NO3 as ligands. Active as Lysozyme, with EC number 3.2.1.17 Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9 and BC1. 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
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Categories: Gallus gallus | Lysozyme | Single protein | Broutin, I. | Ducruix, A. | Ries-Kautt, M. | Vaney, M.C. | NA | NO3 | Hydrolase | Hydrolase (o-glycosyl)
