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| | <StructureSection load='1lmn' size='340' side='right'caption='[[1lmn]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1lmn' size='340' side='right'caption='[[1lmn]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1lmn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oncmy Oncmy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LMN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1lmn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LMN FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmn OCA], [https://pdbe.org/1lmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lmn RCSB], [https://www.ebi.ac.uk/pdbsum/1lmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmn ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmn OCA], [https://pdbe.org/1lmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lmn RCSB], [https://www.ebi.ac.uk/pdbsum/1lmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LYSC2_ONCMY LYSC2_ONCMY]] 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. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.<ref>PMID:15142536</ref>
| + | [https://www.uniprot.org/uniprot/LYSC2_ONCMY LYSC2_ONCMY] 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. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.<ref>PMID:15142536</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/1lmn_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/1lmn_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]] | + | [[Category: Oncorhynchus mykiss]] |
| - | [[Category: Oncmy]]
| + | [[Category: Hough E]] |
| - | [[Category: Hough, E]] | + | [[Category: Karlsen S]] |
| - | [[Category: Karlsen, S]] | + | |
| Structural highlights
Function
LYSC2_ONCMY 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. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.[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 PubMed
Lysozymes (E.C. 3.2.1.17) are well characterized ubiquitous enzymes that have an antibacterial effect. The lysozymes from rainbow trout (RBTL) (Oncorhynchus mykiss) could be particularly interesting in aquaculture since they show higher activity than egg-white lysozyme and lysozymes from other fish species against a variety of pathogenic bacteria. Two lysozymes, I and II, differing only in a single amino acid, were purified from the kidney of rainbow trout and shown to belong to the c-type class of lysozymes. The type II form was shown to be much more potent against a variety of bacteria than the type I enzyme. We have grown crystals from a mixture containing about 80% type I and 20% type II lysozyme from rainbow trout, and solved the X-ray crystal structure. The crystals are trigonal with a = 76.68, c = 54.46 A and space group P3(1)21. The phase problem was solved by the molecular-replacement method, and the structure was refined to an R-factor of 17.4% using data to 1.8 A resolution. The crystal structure shows that the three-dimensional structure of rainbow trout lysozyme is very similar to the previously solved structures of other c-type lysozymes. The single polypeptide of 129 amino acids is folded into two domains separated by a deep cleft which contains the active site. Secondary-structure elements, four alpha-helices and a three-stranded beta-sheet, are located in the same sequential positions as in the hen, turkey and human enzymes. The beta-sheet is found to be common for structures of both c- and g-type lysozymes. We suggest that differences in antibiotic activity of the two forms of RBTL are probably due to small differences in the hydophobicity of a small surface region.
Refined crystal structure of lysozyme from the rainbow trout (Oncorhynchus mykiss).,Karlsen S, Eliassen BE, Hansen LK, Larsen RL, Riise BW, Smalas AO, Hough E, Grinde B Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):354-67. PMID:15299303[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fernandes JM, Kemp GD, Smith VJ. Two novel muramidases from skin mucosa of rainbow trout (Oncorhynchus mykiss). Comp Biochem Physiol B Biochem Mol Biol. 2004 May;138(1):53-64. PMID:15142536 doi:http://dx.doi.org/10.1016/j.cbpc.2004.02.004
- ↑ Karlsen S, Eliassen BE, Hansen LK, Larsen RL, Riise BW, Smalas AO, Hough E, Grinde B. Refined crystal structure of lysozyme from the rainbow trout (Oncorhynchus mykiss). Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):354-67. PMID:15299303 doi:10.1107/S0907444994010929
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