1VE6

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1

Summary for 1VE6

• Entry DOI: 10.2210/pdb1ve6/pdb
• Related: 1VE7
• Descriptor: Acylamino-acid-releasing enzyme, octyl beta-D-glucopyranoside, GLYCEROL, ... (4 entities in total)
• Functional Keywords: beta propeller domain, alpha/beta hydrolase domain, hydrolase
• Biological source: Aeropyrum pernix
• Total number of polymer chains: 2
• Total formula weight: 126986.03

Authors

Bartlam, M.,Wang, G.,Gao, R.,Yang, H.,Zhao, X.,Xie, G.,Cao, S.,Feng, Y.,Rao, Z. (deposition date: 2004-03-27, release date: 2004-11-02, Last modification date: 2024-10-16)

Primary citation

Bartlam, M.,Wang, G.,Yang, H.,Gao, R.,Zhao, X.,Xie, G.,Cao, S.,Feng, Y.,Rao, Z.
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1
STRUCTURE, 12:1481-1488, 2004

PubMed Abstract: 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.

PubMed: 15296741
DOI: 10.1016/j.str.2004.05.019

Experimental method

X-RAY DIFFRACTION (2.1 Å)