2IW0
Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum
Summary for 2IW0
| Entry DOI | 10.2210/pdb2iw0/pdb |
| Descriptor | CHITIN DEACETYLASE, ZINC ION, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | hydrolase, chitin de-n-acetylase, family 4 carbohydrate esterase |
| Biological source | COLLETOTRICHUM LINDEMUTHIANUM (GLOMERELLA LINDEMUTHIANA) |
| Total number of polymer chains | 1 |
| Total formula weight | 28277.01 |
| Authors | Blair, D.E.,Hekmat, O.,Schuttelkopf, A.W.,Shrestha, B.,Tokuyasu, K.,Withers, S.G.,van Aalten, D.M.F. (deposition date: 2006-06-23, release date: 2006-07-04, Last modification date: 2024-10-09) |
| Primary citation | Blair, D.E.,Hekmat, O.,Schuttelkopf, A.W.,Shrestha, B.,Tokuyasu, K.,Withers, S.G.,Van Aalten, D.M.F. Structure and Mechanism of Chitin Deacetylase from the Fungal Pathogen Colletotrichum Lindemuthianum. Biochemistry, 45:9416-, 2006 Cited by PubMed Abstract: The fungal pathogen Colletotrichum lindemuthianum secretes an endo-chitin de-N-acetylase (ClCDA) to modify exposed hyphal chitin during penetration and infection of plants. Although a significant amount of biochemical data is available on fungal chitin de-N-acetylases, no structural data exist. Here we describe the 1.8 A crystal structure of a ClCDA product complex and the analysis of the reaction mechanism using Hammett linear free energy relationships, subsite probing, and atomic absorption spectroscopy studies. The structural data in combination with biochemical data reveal that ClCDA consists of a single domain encompassing a mononuclear metalloenzyme which employs a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The data presented here indicate that ClCDA possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Strikingly, the structure also shows that the hexahistidine purification tag appears to form a tight interaction with the active site groove. The enzyme requires occupancy of at least the 0 and +1 subsites by (GlcNAc)(2) for activity and proceeds through a tetrahedral oxyanion intermediate. PubMed: 16878976DOI: 10.1021/BI0606694 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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