1ivm
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ivm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivm OCA], [http://www.ebi.ac.uk/pdbsum/1ivm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ivm RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:25:16 2008'' |
Revision as of 18:25, 30 March 2008
| |||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of mouse lysozyme M
Overview
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 Structure
1IVM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 21:25:16 2008
Categories: Lysozyme | Mus musculus | Single protein | Imoto, T. | Obita, T. | Ueda, T. | Glycosidase | Hydrolase
