1IVM
Solution structure of mouse lysozyme M
Summary for 1IVM
| Entry DOI | 10.2210/pdb1ivm/pdb |
| NMR Information | BMRB: 4751 |
| Descriptor | lysozyme M (1 entity in total) |
| Functional Keywords | hydrolase, glycosidase |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Secreted: P08905 |
| Total number of polymer chains | 1 |
| Total formula weight | 14839.64 |
| Authors | |
| Primary citation | Obita, T.,Ueda, T.,Imoto, T. Solution structure and activity of mouse lysozyme M CELL.MOL.LIFE SCI., 60:176-184, 2003 Cited by PubMed Abstract: 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. PubMed: 12613666DOI: 10.1007/s000180300012 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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