2X8R
The structure of a family GH25 lysozyme from Aspergillus fumigatus
Summary for 2X8R
| Entry DOI | 10.2210/pdb2x8r/pdb |
| Descriptor | GLYCOSYL HYDROLASE, CHLORIDE ION (3 entities in total) |
| Functional Keywords | peptidoglycan cleavage, endo-n-acetylmuramidases, hydrolase, dxe motif |
| Biological source | ASPERGILLUS FUMIGATUS |
| Total number of polymer chains | 6 |
| Total formula weight | 140517.00 |
| Authors | Korczynska, J.E.,Danielsen, S.,Schagerlof, U.,Turkenburg, J.P.,Davies, G.J.,Wilson, K.S.,Taylor, E.J. (deposition date: 2010-03-11, release date: 2010-09-08, Last modification date: 2024-10-09) |
| Primary citation | Korczynska, J.E.,Danielsen, S.,Schagerlof, U.,Turkenburg, J.P.,Davies, G.J.,Wilson, K.S.,Taylor, E.J. The Structure of a Family Gh25 Lysozyme from Aspergillus Fumigatus Acta Crystallogr.,Sect.F, 66:973-, 2010 Cited by PubMed Abstract: Lysins are important biomolecules which cleave the bacterial cell-wall polymer peptidoglycan. They are finding increasing commercial and medical application. In order to gain an insight into the mechanism by which these enzymes operate, the X-ray structure of a CAZy family GH25 ;lysozyme' from Aspergillus fumigatus was determined. This is the first fungal structure from the family and reveals a modified alpha/beta-barrel-like fold in which an eight-stranded beta-barrel is flanked by three alpha-helices. The active site lies toward the bottom of a negatively charged pocket and its layout has much in common with other solved members of the GH25 and related GH families. A conserved active-site DXE motif may be implicated in catalysis, lending further weight to the argument that this glycoside hydrolase family operates via a ;substrate-assisted' catalytic mechanism. PubMed: 20823508DOI: 10.1107/S1744309110025601 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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