1UKC
Crystal Structure of Aspergillus niger EstA
Summary for 1UKC
| Entry DOI | 10.2210/pdb1ukc/pdb |
| Descriptor | EstA, alpha-D-mannopyranose-(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, ... (9 entities in total) |
| Functional Keywords | esterase, fungi, a/b hydrolase fold, acetylcholinesterase, hydrolase |
| Biological source | Aspergillus niger |
| Total number of polymer chains | 2 |
| Total formula weight | 118464.99 |
| Authors | Bourne, Y.,Hasper, A.A.,Chahinian, H.,Juin, M.,De Graaff, L.H.,Marchot, P. (deposition date: 2003-08-19, release date: 2004-07-27, Last modification date: 2024-10-23) |
| Primary citation | Bourne, Y.,Hasper, A.A.,Chahinian, H.,Juin, M.,De Graaff, L.H.,Marchot, P. Aspergillus niger protein EstA defines a new class of fungal esterases within the alpha/beta hydrolase fold superfamily of proteins STRUCTURE, 12:677-687, 2004 Cited by PubMed Abstract: From the fungus Aspergillus niger, we identified a new gene encoding protein EstA, a member of the alpha/beta-hydrolase fold superfamily but of unknown substrate specificity. EstA was overexpressed and its crystal structure was solved by molecular replacement using a lipase-acetylcholinesterase chimera template. The 2.1 A resolution structure of EstA reveals a canonical Ser/Glu/His catalytic triad located in a small pocket at the bottom of a large solvent-accessible, bowl-shaped cavity. Potential substrates selected by manual docking procedures were assayed for EstA activity. Consistent with the pocket geometry, preference for hydrolysis of short acyl/propyl chain substrates was found. Identification of close homologs from the genome of other fungi, of which some are broad host-range pathogens, defines EstA as the first member of a novel class of fungal esterases within the superfamily. Hence the structure of EstA constitutes a lead template in the design of new antifungal agents directed toward its pathogenic homologs. PubMed: 15062090DOI: 10.1016/j.str.2004.03.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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