2bq8

From Proteopedia

Revision as of 14:40, 30 October 2007

CRYSTAL STRUCTURE OF HUMAN PURPLE ACID PHOSPHATASE WITH AN INHIBITORY CONFORMATION OF THE REPRESSION LOOP

Overview

The crystal structure of human purple acid phosphatase recombinantly, expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)), has been determined in two different crystal forms, both at 2.2A, resolution. In both cases, the enzyme crystallized in its oxidized, (inactive) state, in which both Fe atoms in the dinuclear active site are, Fe(III). The main difference between the two structures is the, conformation of the enzyme "repression loop". Proteolytic cleavage of this, loop in vivo or in vitro results in significant activation of the, mammalian PAPs. In the crystals obtained from rHPAP(Ec), the carboxylate, side-chain of Asp145 of this loop acts as a bidentate ligand that bridges, the two metal atoms, in a manner analogous to a possible binding mode for, a phosphate ... [(full description)]

About this Structure

2BQ8 is a [Single protein] structure of sequence from [Homo sapiens] with FE2, ZN and SO4 as [ligands]. Active as [Acid phosphatase], with EC number [3.1.3.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop., Strater N, Jasper B, Scholte M, Krebs B, Duff AP, Langley DB, Han R, Averill BA, Freeman HC, Guss JM, J Mol Biol. 2005 Aug 5;351(1):233-46. Epub 2005 Apr 26. PMID:15993892

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