Summary for 6IBW
| Entry DOI | 10.2210/pdb6ibw/pdb |
| Related | 6IBU |
| Descriptor | Probable glycosidase crf1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | cross-link, transglycosylase, gh16, cell wall assembly, hydrolase |
| Biological source | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Total number of polymer chains | 2 |
| Total formula weight | 55704.65 |
| Authors | Fang, W.,Bartual, S.G.,van Aalten, D.M.F. (deposition date: 2018-12-01, release date: 2019-02-27, Last modification date: 2024-11-13) |
| Primary citation | Fang, W.,Sanz, A.B.,Bartual, S.G.,Wang, B.,Ferenbach, A.T.,Farkas, V.,Hurtado-Guerrero, R.,Arroyo, J.,van Aalten, D.M.F. Mechanisms of redundancy and specificity of the Aspergillus fumigatus Crh transglycosylases. Nat Commun, 10:1669-1669, 2019 Cited by PubMed Abstract: Fungal cell wall synthesis is achieved by a balance of glycosyltransferase, hydrolase and transglycosylase activities. Transglycosylases strengthen the cell wall by forming a rigid network of crosslinks through mechanisms that remain to be explored. Here we study the function of the Aspergillus fumigatus family of five Crh transglycosylases. Although crh genes are dispensable for cell viability, simultaneous deletion of all genes renders cells sensitive to cell wall interfering compounds. In vitro biochemical assays and localisation studies demonstrate that this family of enzymes functions redundantly as transglycosylases for both chitin-glucan and chitin-chitin cell wall crosslinks. To understand the molecular basis of this acceptor promiscuity, we solved the crystal structure of A. fumigatus Crh5 (AfCrh5) in complex with a chitooligosaccharide at the resolution of 2.8 Å, revealing an extensive elongated binding cleft for the donor (-4 to -1) substrate and a short acceptor (+1 to +2) binding site. Together with mutagenesis, the structure suggests a "hydrolysis product assisted" molecular mechanism favouring transglycosylation over hydrolysis. PubMed: 30971696DOI: 10.1038/s41467-019-09674-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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