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 | |
| 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 Cited by 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: 15296741DOI: 10.1016/j.str.2004.05.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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