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6ZMV

Structure of muramidase from Trichobolus zukalii

Summary for 6ZMV
Entry DOI10.2210/pdb6zmv/pdb
Descriptormuramidase, GLYCEROL, SULFATE ION, ... (4 entities in total)
Functional Keywordsmuramidase, fungal, gh25, lysozyme, industrial application, peptidoglycan cleavage, hydrolase
Biological sourceTrichobolus zukalii
Total number of polymer chains2
Total formula weight46012.64
Authors
Primary citationMoroz, 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: 33711051
DOI: 10.1371/journal.pone.0248190
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

226707

數據於2024-10-30公開中

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