3N2W

Crystal structure of the N-terminal beta-aminopeptidase BapA from Sphingosinicella xenopeptidilytica

3N2W の概要

• エントリーDOI: 10.2210/pdb3n2w/pdb
• 関連するPDBエントリー: 3N33 3N5I
• 分子名称: Beta-peptidyl aminopeptidase, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ntn hydrolase, alpha-beta-beta-alpha sandwich, beta-aminopeptidase, beta-peptide, hydrolase
• 由来する生物種: Sphingosinicella xenopeptidilytica
• 細胞内の位置: Periplasm : Q52VH2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 155948.54

構造登録者

Merz, T.,Heck, T.,Geueke, B.,Kohler, H.-P.,Gruetter, M.G. (登録日: 2010-05-19, 公開日: 2011-06-08, 最終更新日: 2023-09-06)

主引用文献

Merz, T.,Heck, T.,Geueke, B.,Mittl, P.R.,Briand, C.,Seebach, D.,Kohler, H.P.,Grutter, M.G.
Autoproteolytic and catalytic mechanisms for the beta-aminopeptidase BapA--a member of the Ntn hydrolase family.
Structure, 20:1850-1860, 2012

PubMed Abstract: The β-aminopeptidase BapA from Sphingosinicella xenopeptidilytica belongs to the N-terminal nucleophile (Ntn) hydrolases of the DmpA-like family and has the unprecedented property of cleaving N-terminal β-amino acid residues from peptides. We determined the crystal structures of the native (αβ)₄ heterooctamer and of the 153 kDa precursor homotetramer at a resolution of 1.45 and 1.8 Å, respectively. These structures together with mutational analyses strongly support mechanisms for autoproteolysis and catalysis that involve residues Ser250, Ser288, and Glu290. The autoproteolytic mechanism is different from the one so far described for Ntn hydrolases. The structures together with functional data also provide insight into the discriminating features of the active site cleft that determine substrate specificity.

PubMed: 22980995
DOI: 10.1016/j.str.2012.07.017

実験手法

X-RAY DIFFRACTION (1.45 Å)