3N2W

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

Summary for 3N2W

• Entry DOI: 10.2210/pdb3n2w/pdb
• Related: 3N33 3N5I
• Descriptor: Beta-peptidyl aminopeptidase, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ntn hydrolase, alpha-beta-beta-alpha sandwich, beta-aminopeptidase, beta-peptide, hydrolase
• Biological source: Sphingosinicella xenopeptidilytica
• Cellular location: Periplasm : Q52VH2
• Total number of polymer chains: 4
• Total formula weight: 155948.54

Authors

Merz, T.,Heck, T.,Geueke, B.,Kohler, H.-P.,Gruetter, M.G. (deposition date: 2010-05-19, release date: 2011-06-08, Last modification date: 2023-09-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.45 Å)