8b2h: Difference between revisions
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==Muramidase from Thermothielavioides terrestris, catalytic domain== | |||
<StructureSection load='8b2h' size='340' side='right'caption='[[8b2h]], [[Resolution|resolution]] 2.36Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8b2h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothielavioides_terrestris Thermothielavioides terrestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8B2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B2H 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]] 2.36Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8b2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b2h OCA], [https://pdbe.org/8b2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b2h RCSB], [https://www.ebi.ac.uk/pdbsum/8b2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b2h ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G2QV10_THETT G2QV10_THETT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Muramidases (also known as lysozymes) hydrolyse the peptidoglycan component of the bacterial cell wall and are found in many glycoside hydrolase (GH) families. Similar to other glycoside hydrolases, muramidases sometimes have noncatalytic domains that facilitate their interaction with the substrate. Here, the identification, characterization and X-ray structure of a novel fungal GH24 muramidase from Trichophaea saccata is first described, in which an SH3-like cell-wall-binding domain (CWBD) was identified by structure comparison in addition to its catalytic domain. Further, a complex between a triglycine peptide and the CWBD from T. saccata is presented that shows a possible anchor point of the peptidoglycan on the CWBD. A ;domain-walking' approach, searching for other sequences with a domain of unknown function appended to the CWBD, was then used to identify a group of fungal muramidases that also contain homologous SH3-like cell-wall-binding modules, the catalytic domains of which define a new GH family. The properties of some representative members of this family are described as well as X-ray structures of the independent catalytic and SH3-like domains of the Kionochaeta sp., Thermothielavioides terrestris and Penicillium virgatum enzymes. This work confirms the power of the module-walking approach, extends the library of known GH families and adds a new noncatalytic module to the muramidase arsenal. | |||
Module walking using an SH3-like cell-wall-binding domain leads to a new GH184 family of muramidases.,Moroz OV, Blagova E, Lebedev AA, Skov LK, Pache RA, Schnorr KM, Kiemer L, Friis EP, Nymand-Grarup S, Ming L, Ye L, Klausen M, Cohn MT, Schmidt EGW, Davies GJ, Wilson KS Acta Crystallogr D Struct Biol. 2023 Aug 1. doi: 10.1107/S2059798323005004. PMID:37428847<ref>PMID:37428847</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8b2h" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermothielavioides terrestris]] | ||
[[Category: | [[Category: Blagova E]] | ||
[[Category: | [[Category: Cohn MT]] | ||
[[Category: | [[Category: Davies GJ]] | ||
[[Category: | [[Category: Kiemer L]] | ||
[[Category: | [[Category: Klausen M]] | ||
[[Category: | [[Category: Lebedev AA]] | ||
[[Category: | [[Category: Ming L]] | ||
[[Category: | [[Category: Moroz OV]] | ||
[[Category: Nymand-Grarup S]] | |||
[[Category: Pache RA]] | |||
[[Category: Schmidt EGW]] | |||
[[Category: Schnorr KM]] | |||
[[Category: Skov LK]] | |||
[[Category: Wilson KS]] | |||
[[Category: Ye L]] | |||
Revision as of 09:11, 19 July 2023
Muramidase from Thermothielavioides terrestris, catalytic domainMuramidase from Thermothielavioides terrestris, catalytic domain
Structural highlights
FunctionPublication Abstract from PubMedMuramidases (also known as lysozymes) hydrolyse the peptidoglycan component of the bacterial cell wall and are found in many glycoside hydrolase (GH) families. Similar to other glycoside hydrolases, muramidases sometimes have noncatalytic domains that facilitate their interaction with the substrate. Here, the identification, characterization and X-ray structure of a novel fungal GH24 muramidase from Trichophaea saccata is first described, in which an SH3-like cell-wall-binding domain (CWBD) was identified by structure comparison in addition to its catalytic domain. Further, a complex between a triglycine peptide and the CWBD from T. saccata is presented that shows a possible anchor point of the peptidoglycan on the CWBD. A ;domain-walking' approach, searching for other sequences with a domain of unknown function appended to the CWBD, was then used to identify a group of fungal muramidases that also contain homologous SH3-like cell-wall-binding modules, the catalytic domains of which define a new GH family. The properties of some representative members of this family are described as well as X-ray structures of the independent catalytic and SH3-like domains of the Kionochaeta sp., Thermothielavioides terrestris and Penicillium virgatum enzymes. This work confirms the power of the module-walking approach, extends the library of known GH families and adds a new noncatalytic module to the muramidase arsenal. Module walking using an SH3-like cell-wall-binding domain leads to a new GH184 family of muramidases.,Moroz OV, Blagova E, Lebedev AA, Skov LK, Pache RA, Schnorr KM, Kiemer L, Friis EP, Nymand-Grarup S, Ming L, Ye L, Klausen M, Cohn MT, Schmidt EGW, Davies GJ, Wilson KS Acta Crystallogr D Struct Biol. 2023 Aug 1. doi: 10.1107/S2059798323005004. PMID:37428847[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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