6zm8: Difference between revisions

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== Structural highlights ==

<table><tr><td colspan='2'>~~[[6zm8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sodiomyces_alcalophilus Sodiomyces alcalophilus].~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZM8 FirstGlance]. <br>

<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZM8 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]] 0.78Å</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=6zm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zm8 OCA], [https://pdbe.org/6zm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zm8 RCSB], [https://www.ebi.ac.uk/pdbsum/6zm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zm8 ProSAT]</span></td></tr>

</table>

~~== Function ==~~

~~[https://www.uniprot.org/uniprot/A0A7S6K8E4_SODAL A0A7S6K8E4_SODAL]~~

~~<div style="background-color:#fffaf0;">~~

~~== Publication Abstract from PubMed ==~~

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.

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>

~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~

~~</div>~~

~~<div class="pdbe-citations 6zm8" style="background-color:#fffaf0;"></div>~~

~~== References ==~~

~~<references/>~~

__TOC__

</StructureSection>

[[Category: Large Structures]]

~~[[Category: Sodiomyces alcalophilus]]~~

[[Category: Blagova E]]

[[Category: Cohn MT]]

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@@ Line 3: / Line 3: @@
 <StructureSection load='6zm8' size='340' side='right'caption='[[6zm8]], [[Resolution|resolution]] 0.78&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6zm8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sodiomyces_alcalophilus Sodiomyces alcalophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZM8 FirstGlance]. <br>
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZM8 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]] 0.78&#8491;</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=6zm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zm8 OCA], [https://pdbe.org/6zm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zm8 RCSB], [https://www.ebi.ac.uk/pdbsum/6zm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zm8 ProSAT]</span></td></tr>
 </table>
-== Function ==
-[https://www.uniprot.org/uniprot/A0A7S6K8E4_SODAL A0A7S6K8E4_SODAL]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6zm8" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Sodiomyces alcalophilus]]
 [[Category: Blagova E]]
 [[Category: Cohn MT]]