Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1IVM

Solution structure of mouse lysozyme M

Summary for 1IVM
Entry DOI10.2210/pdb1ivm/pdb
NMR InformationBMRB: 4751
Descriptorlysozyme M (1 entity in total)
Functional Keywordshydrolase, glycosidase
Biological sourceMus musculus (house mouse)
Cellular locationSecreted: P08905
Total number of polymer chains1
Total formula weight14839.64
Authors
Ueda, T.,Obita, T.,Imoto, T. (deposition date: 2002-03-27, release date: 2002-05-08, Last modification date: 2024-10-30)
Primary citationObita, 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: 12613666
DOI: 10.1007/s000180300012
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon