1ivm
Solution structure of mouse lysozyme M
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OverviewOverview
The three-dimensional structure of mouse lysozyme M, glycoside hydrolase, with 130 amino acids has been determined by heteronuclear NMR, spectroscopy. We found that mouse lysozyme M had four alpha-helices, two, 3(10)helices, and a double- and a triple-stranded anti-parallel, beta-sheet, and its structure was very similar to that of hen lysozyme in, solution and in the crystalline state. The pH activity profile of, p-nitrophenyl penta N-acetyl-beta-D-chitopentaoside hydrolysis by mouse, lysozyme M was similar to that of hen lysozyme, but the hydrolytic, activity of mouse lysozyme M was lower. From analyses of binding, affinities of lysozymes to a substrate analogue and internal motions of, lysozymes, we suggest that the lower activity of mouse lysozyme M was due, to the larger dissociation constant of its enzyme-substrate complex and, the restricted internal backbone motions in the molecule.
About this StructureAbout this Structure
1IVM is a Single protein structure of sequence from Mus musculus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Solution structure and activity of mouse lysozyme M., Obita T, Ueda T, Imoto T, Cell Mol Life Sci. 2003 Jan;60(1):176-84. PMID:12613666
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