PDBsum entry 3n33

Hydrolase/hydrolase inhibitor

PDB id: 3n33

Contents

Protein chains

367 a.a.

Ligands

GOL ×4

EPE ×2

AES ×8

SO4 ×16

Waters ×1265

PDB id:

3n33

Name:

Hydrolase/hydrolase inhibitor

Title:

Crystal structure of the n-terminal beta-aminopeptidase bapa in complex with pefabloc sc (aebsf)

Structure:

Beta-peptidyl aminopeptidase. Chain: a, b, c, d. Engineered: yes

Source:

Sphingosinicella xenopeptidilytica. Organism_taxid: 364098. Gene: bapa. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.80Å R-factor: 0.160 R-free: 0.191

Authors:

T.Merz,T.Heck,B.Geueke,H.-P.Kohler,M.G.Gruetter

Key ref:

T.Merz et al. (2012). Autoproteolytic and catalytic mechanisms for the β-aminopeptidase BapA--a member of the Ntn hydrolase family. Structure, 20, 1850-1860. PubMed id: 22980995

Date:

19-May-10 Release date: 08-Jun-11

Protein chains

Q52VH2  (BAPA_SPHXN) -  Beta-peptidyl aminopeptidase BapA from Sphingosinicella xenopeptidilytica

Seq: 402 a.a.

Struc: 367 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.11.25 - beta-peptidyl aminopeptidase.

Structure 20:1850-1860 (2012)

PubMed id: 22980995

Autoproteolytic and catalytic mechanisms for the β-aminopeptidase BapA--a member of the Ntn hydrolase family.

T.Merz, T.Heck, B.Geueke, P.R.Mittl, C.Briand, D.Seebach, H.P.Kohler, M.G.Grütter.

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.