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| <StructureSection load='6zmv' size='340' side='right'caption='[[6zmv]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='6zmv' size='340' side='right'caption='[[6zmv]], [[Resolution|resolution]] 1.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6zmv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thelebolus_zukalii Thelebolus zukalii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZMV FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZMV FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.4Å</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> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6zmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zmv OCA], [https://pdbe.org/6zmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zmv RCSB], [https://www.ebi.ac.uk/pdbsum/6zmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zmv 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=6zmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zmv OCA], [https://pdbe.org/6zmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zmv RCSB], [https://www.ebi.ac.uk/pdbsum/6zmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zmv ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Muramidases/lysozymes hydrolyse the peptidoglycan component of the bacterial cell wall. They are found in many of the glycoside hydrolase (GH) families. Family GH25 contains muramidases/lysozymes, known as CH type lysozymes, as they were initially discovered in the Chalaropsis species of fungus. The characterized enzymes from GH25 exhibit both beta-1,4-N-acetyl- and beta-1,4-N,6-O-diacetylmuramidase activities, cleaving the beta-1,4-glycosidic bond between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) moieties in the carbohydrate backbone of bacterial peptidoglycan. Here, a set of fungal GH25 muramidases were identified from a sequence search, cloned and expressed and screened for their ability to digest bacterial peptidoglycan, to be used in a commercial application in chicken feed. The screen identified the enzyme from Acremonium alcalophilum JCM 736 as a suitable candidate for this purpose and its relevant biochemical and biophysical and properties are described. We report the crystal structure of the A. alcalophilum enzyme at atomic, 0.78 A resolution, together with that of its homologue from Trichobolus zukalii at 1.4 A, and compare these with the structures of homologues. GH25 enzymes offer a new solution in animal feed applications such as for processing bacterial debris in the animal gut.
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| Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78A resolution.,Moroz OV, Blagova E, Taylor E, Turkenburg JP, Skov LK, Gippert GP, Schnorr KM, Ming L, Ye L, Klausen M, Cohn MT, Schmidt EGW, Nymand-Grarup S, Davies GJ, Wilson KS PLoS One. 2021 Mar 12;16(3):e0248190. doi: 10.1371/journal.pone.0248190., eCollection 2021. PMID:33711051<ref>PMID:33711051</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6zmv" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Lysozyme]]
| | [[Category: Blagova E]] |
| [[Category: Thelebolus zukalii]]
| | [[Category: Cohn MT]] |
| [[Category: Blagova, E]] | | [[Category: Davies GJ]] |
| [[Category: Cohn, M T]] | | [[Category: Gippert GP]] |
| [[Category: Davies, G J]] | | [[Category: Klausen M]] |
| [[Category: Gippert, G P]] | | [[Category: Ming L]] |
| [[Category: Klausen, M]] | | [[Category: Moroz OV]] |
| [[Category: Ming, L]] | | [[Category: Nymand-Grarup S]] |
| [[Category: Moroz, O V]] | | [[Category: Schmidt EGW]] |
| [[Category: Nymand-Grarup, S]] | | [[Category: Schnorr KM]] |
| [[Category: Schmidt, E G.W]] | | [[Category: Skov LK]] |
| [[Category: Schnorr, K M]] | | [[Category: Taylor E]] |
| [[Category: Skov, L K]] | | [[Category: Turkenburg JP]] |
| [[Category: Taylor, E]] | | [[Category: Wilson KS]] |
| [[Category: Turkenburg, J P]] | | [[Category: Ye L]] |
| [[Category: Wilson, K S]] | |
| [[Category: Ye, L]] | |
| [[Category: Fungal]]
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| [[Category: Gh25]]
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| [[Category: Hydrolase]]
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| [[Category: Industrial application]]
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| [[Category: Muramidase]]
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| [[Category: Peptidoglycan cleavage]]
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