1ivm: Difference between revisions
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[[Image:1ivm.gif|left|200px]] | [[Image:1ivm.gif|left|200px]] | ||
'''Solution structure of mouse lysozyme M''' | {{Structure | ||
|PDB= 1ivm |SIZE=350|CAPTION= <scene name='initialview01'>1ivm</scene> | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''Solution structure of mouse lysozyme M''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IVM is a [ | 1IVM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVM OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12613666 12613666] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:55:28 2008'' | ||
Revision as of 12:55, 20 March 2008
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| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of mouse lysozyme M
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. 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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