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J Mol Biol. 1999 May 21;288(5):965-74.

Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution.

Author information

1
F. Hoffmann-La Roche Ltd, B/65/R312, Basel, 4070, Switzerland. dirk.kostrewa@roche.com

Abstract

The crystal structure of Aspergillus niger pH 2.5 acid phosphatase (EC 3.1.3.2) has been determined at 2.4 A resolution. In the crystal, two dimers form a tetramer in which the active sites are easily accessible to substrates. The main contacts in the dimer come from the N termini, each lying on the surface of the neighbouring molecule. The monomer consists of two domains, with the active site located at their interface. The active site has a highly conserved catalytic center and a charge distribution, which explains the highly acidic pH optimum and the broad substrate specificity of the enzyme.

PMID:
10329192
DOI:
10.1006/jmbi.1999.2736
[Indexed for MEDLINE]
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