1lkr | pdb_00001lkr

MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE

spinqualitylabelsall models 1lkr, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lkr is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: IOD 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Hen egg-white lysozyme is one of the most thoroughly studied of enzymes and has been the subject of study by many methods, including X-ray crystallography. The present work extends the X-ray crystallography to higher resolution, includes the positions of the anions, and examines the contacts of the neighbors in greater detail. Data were collected at room temperature on a Rigaku R-axis area detector with rotating-anode X-ray generator to 1.6 A resolution for monoclinic lysozyme iodide at pH 4.0, to 1.8 A for monoclinic lysozyme iodide at pH 8.0, and to 1.1 A resolution for triclinic lysozyme nitrate at pH 4.5. The structures have been refined by SHELX93 with the expected number of anion sites being accounted for. Two regions of the protein have been found to be variable: residues 65-75 and 99-104. Except for 65-75 and 99-104, lysozyme is a very stable molecule with the crystal forms being held together by the electrostatic contacts of the anions and by layers of water molecules. The anion positions can be described as paired half sites, each half being contributed by a different lysozyme molecule. The many different crystal forms of lysozyme may be due to different combinations of the many such half sites on the surface. A hypothesis is presented for lysozyme in the different crystal forms and which may be extended to behavior in solution. Suggestions for future crystallographic research are proposed, involving anions of different shape and charge. Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic lysozyme nitrate at 1.1 A.,Steinrauf LK Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):767-80. PMID:9757091 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysozyme 3D structures

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