Crystal Structure of Prolyl Aminopeptidase from Serratia marcescens

• Published in: Journal of biochemistry (Tokyo) 1999-09, Vol.126 (3), p.559-565
• Main Authors: Yoshimoto, Tadashi, Kabashima, Tsutomu, Uchikawa, Kouichirou, Inoue, Takahiko, Tanaka, Nobutada, Nakamura, Razuo T., Tsuru, Masato, Ito, Eiyoshi
• Format: Article
• Language: English
• Subjects: Aminopeptidases - chemistry; Aminopeptidases - metabolism; Binding Sites; Crystallography, X-Ray; Cysteine - chemistry; Cysteine - metabolism; Models, Molecular; proline; proline iminopeptidase; prolyl aminopeptidase; Protein Conformation; Serratia marcescens; Serratia marcescens - enzymology; Substrate Specificity; X-ray analysis; α/β hydrolase
• ISSN: 0021-924X
• DOI: 10.1093/oxfordjournals.jbchem.a022486

Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the removal of N-terminal proline residues from pep tides. We have solved its three-dimensional structure at 2.3 Å resolution by the multiple isomorphous replacement method. The enzyme consists of two contiguous domains. The larger domain shows the general topology of the α/β hydrolase fold, with a central eight-stranded β-sheet and six helices. The smaller domain consists of six helices. The catalytic triad (Serll3, Hi8296, and Asp268) is located near the large cavity at the interface between the two domains. Cys271, which is sensitive to SH reagents, is located near the catalytic residues, in spite of the fact that the enzyme is a serine peptidase. The specific residues which make up the hydrophobic pocket line the smaller domain, and the specificity of the exo-type enzyme originates from this smaller domain, which blocks the N-terminal of P1 proline.