6ZMV
Structure of muramidase from Trichobolus zukalii
Summary for 6ZMV
| Entry DOI | 10.2210/pdb6zmv/pdb |
| Descriptor | muramidase, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | muramidase, fungal, gh25, lysozyme, industrial application, peptidoglycan cleavage, hydrolase |
| Biological source | Trichobolus zukalii |
| Total number of polymer chains | 2 |
| Total formula weight | 46012.64 |
| Authors | Moroz, O.V.,Blagova, E.,Taylor, E.,Turkenburg, J.P.,Skov, L.K.,Gippert, G.P.,Schnorr, K.M.,Ming, L.,Ye, L.,Klausen, M.,Cohn, M.T.,Schmidt, E.G.W.,Nymand-Grarup, S.,Davies, G.J.,Wilson, K.S. (deposition date: 2020-07-04, release date: 2021-07-14, Last modification date: 2024-11-06) |
| Primary citation | Moroz, O.V.,Blagova, E.,Taylor, E.,Turkenburg, J.P.,Skov, L.K.,Gippert, G.P.,Schnorr, K.M.,Ming, L.,Ye, L.,Klausen, M.,Cohn, M.T.,Schmidt, E.G.W.,Nymand-Grarup, S.,Davies, G.J.,Wilson, K.S. Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78 angstrom resolution. Plos One, 16:e0248190-e0248190, 2021 Cited by PubMed Abstract: 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 β-1,4-N-acetyl- and β-1,4-N,6-O-diacetylmuramidase activities, cleaving the β-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 Å resolution, together with that of its homologue from Trichobolus zukalii at 1.4 Å, 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. PubMed: 33711051DOI: 10.1371/journal.pone.0248190 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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