1QTR

CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS

1QTR の概要

• エントリーDOI: 10.2210/pdb1qtr/pdb
• 分子名称: PROLYL AMINOPEPTIDASE (1 entity in total)
• 機能のキーワード: alpha beta hydrolase fold, proline, prolyl aminopeptidase, serratia, iminopeptidase, hydrolase
• 由来する生物種: Serratia marcescens
• 細胞内の位置: Cytoplasm: O32449
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36130.59

構造登録者

Yoshimoto, T.,Kabashima, T.,Uchikawa, K.,Inoue, T.,Tanaka, N. (登録日: 1999-06-28, 公開日: 1999-07-07, 最終更新日: 2024-02-14)

主引用文献

Yoshimoto, T.,Kabashima, T.,Uchikawa, K.,Inoue, T.,Tanaka, N.,Nakamura, K.T.,Tsuru, M.,Ito, K.
Crystal structure of prolyl aminopeptidase from Serratia marcescens.
J.Biochem.(Tokyo), 126:559-565, 1999

PubMed Abstract: Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the removal of N-terminal proline residues from peptides. We have solved its three-dimensional structure at 2.3 A resolution by the multiple isomorphous replacement method. The enzyme consists of two contiguous domains. The larger domain shows the general topology of the alpha/beta hydrolase fold, with a central eight-stranded beta-sheet and six helices. The smaller domain consists of six helices. The catalytic triad (Ser113, His296, 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.

PubMed: 10467172

実験手法

X-RAY DIFFRACTION (2.32 Å)