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== | ==LYSOZYME COMPLEX WITH 4-METHYL-UMBELLIFERYL CHITOTRIOSE== | ||
Two complexes between rainbow trout lysozyme (RBTL) and | <StructureSection load='1bb6' size='340' side='right'caption='[[1bb6]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1bb6]] 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=1BB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BB6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UMG:METHYL-UMBELLIFERTL-N-ACETYL-CHITOTRIOSE'>UMG</scene></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=1bb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bb6 OCA], [https://pdbe.org/1bb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bb6 RCSB], [https://www.ebi.ac.uk/pdbsum/1bb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bb6 ProSAT]</span></td></tr> | |||
</table> | |||
== 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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bb/1bb6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bb6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Two complexes between rainbow trout lysozyme (RBTL) and 4-methylumbelliferyl chitobioside, 4MeU-(GlcNAc)2, and chitotrioside, 4MeU-(GlcNAc)3, were produced by co-crystallization and soaking, respectively, and the crystal structures were solved at 2.0 A resolution. The results show that 4-MeU-(GlcNAc)3 binds in subsites A-D and that 4-MeU-(GlcNAc)2 binds in subsites B-D in the active-site cleft of RBTL. This agrees well with earlier crystallographic studies on the binding of oligosaccharides of chitin to RBTL, which showed that (GlcNAc)3 binds to sites B-D in RBTL and not to A-C as seen in the human and turkey egg-white lysozymes. For both complexes the 4-MeU moiety in site D has diffuse electron density and is flexible, as it is only bound to water molecules and not to the protein. Since no electron density was observed in site E, the solved structures give views of nonproductive enzyme-substrate complexes. | |||
Structural studies on the binding of 4-methylumbelliferone glycosides of chitin to rainbow trout lysozyme.,Vollan VB, Hough E, Karlsen S Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):60-6. Epub 1999 Jan, 1. PMID:10089395<ref>PMID:10089395</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1bb6" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Oncorhynchus mykiss]] | [[Category: Oncorhynchus mykiss]] | ||
[[Category: Hough E]] | |||
[[Category: Hough | [[Category: Karlsen S]] | ||
[[Category: Karlsen | [[Category: Vollan VB]] | ||
[[Category: Vollan | |||
Latest revision as of 10:17, 23 October 2024
LYSOZYME COMPLEX WITH 4-METHYL-UMBELLIFERYL CHITOTRIOSELYSOZYME COMPLEX WITH 4-METHYL-UMBELLIFERYL CHITOTRIOSE
Structural highlights
FunctionLYSC2_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 PubMedTwo complexes between rainbow trout lysozyme (RBTL) and 4-methylumbelliferyl chitobioside, 4MeU-(GlcNAc)2, and chitotrioside, 4MeU-(GlcNAc)3, were produced by co-crystallization and soaking, respectively, and the crystal structures were solved at 2.0 A resolution. The results show that 4-MeU-(GlcNAc)3 binds in subsites A-D and that 4-MeU-(GlcNAc)2 binds in subsites B-D in the active-site cleft of RBTL. This agrees well with earlier crystallographic studies on the binding of oligosaccharides of chitin to RBTL, which showed that (GlcNAc)3 binds to sites B-D in RBTL and not to A-C as seen in the human and turkey egg-white lysozymes. For both complexes the 4-MeU moiety in site D has diffuse electron density and is flexible, as it is only bound to water molecules and not to the protein. Since no electron density was observed in site E, the solved structures give views of nonproductive enzyme-substrate complexes. Structural studies on the binding of 4-methylumbelliferone glycosides of chitin to rainbow trout lysozyme.,Vollan VB, Hough E, Karlsen S Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):60-6. Epub 1999 Jan, 1. PMID:10089395[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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