1ivm: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ivm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVM FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ivm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVM FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1ivm RCSB], [http://www.ebi.ac.uk/pdbsum/1ivm PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1ivm RCSB], [http://www.ebi.ac.uk/pdbsum/1ivm PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/LYZ2_MOUSE LYZ2_MOUSE]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lyz2 is active against a range of Gram-positive and Gram-negative bacteria. More effective than Lyz1 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally effective in killing Gram-positive bacteria.<ref>PMID:14977423</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Imoto, T | [[Category: Imoto, T]] | ||
[[Category: Obita, T | [[Category: Obita, T]] | ||
[[Category: Ueda, T | [[Category: Ueda, T]] | ||
[[Category: Glycosidase]] | [[Category: Glycosidase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 05:58, 25 December 2014
Solution structure of mouse lysozyme MSolution structure of mouse lysozyme M
Structural highlights
Function[LYZ2_MOUSE] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lyz2 is active against a range of Gram-positive and Gram-negative bacteria. More effective than Lyz1 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally effective in killing Gram-positive bacteria.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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