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Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate

Overview

Acylpeptide hydrolases (APH; also known as acylamino acid releasing, enzyme) catalyze the removal of an N-acylated amino acid from blocked, peptides. The crystal structure of an APH from the thermophilic archaeon, Aeropyrum pernix K1 to 2.1 A resolution confirms it to be a member of the, prolyl oligopeptidase family of serine proteases. The structure of apAPH, is a symmetric homodimer with each subunit comprised of two domains. The, N-terminal domain is a regular seven-bladed beta-propeller, while the, C-terminal domain has a canonical alpha/beta hydrolase fold and includes, the active site and a conserved Ser445-Asp524-His556 catalytic triad. The, complex structure of apAPH with an organophosphorus substrate, p-nitrophenyl phosphate, has also been determined. The complex structure, unambiguously maps out the substrate binding pocket and provides a basis, for substrate recognition by apAPH. A conserved mechanism for protein, degradation from archaea to mammals is suggested by the structural, features of apAPH.

About this Structure

1VE7 is a Single protein structure of sequence from Aeropyrum pernix with 4NP and GOL as ligands. Active as Acylaminoacyl-peptidase, with EC number 3.4.19.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1., Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z, Structure. 2004 Aug;12(8):1481-8. PMID:15296741

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