1UKC

Crystal Structure of Aspergillus niger EstA

1UKC の概要

• エントリーDOI: 10.2210/pdb1ukc/pdb
• 分子名称: 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)
• 機能のキーワード: esterase, fungi, a/b hydrolase fold, acetylcholinesterase, hydrolase
• 由来する生物種: Aspergillus niger
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 118464.99

構造登録者

Bourne, Y.,Hasper, A.A.,Chahinian, H.,Juin, M.,De Graaff, L.H.,Marchot, P. (登録日: 2003-08-19, 公開日: 2004-07-27, 最終更新日: 2024-10-23)

主引用文献

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

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: 15062090
DOI: 10.1016/j.str.2004.03.005

実験手法

X-RAY DIFFRACTION (2.1 Å)