3n33 | pdb_00003n33

Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with pefabloc SC (AEBSF)

spinqualitylabelsall models 3n33, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3n33 is a 4 chain structure with sequence from Ccug 52537. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AES, EPE, GOL, SO4 Related: 3n2w, 3n5i Gene: bapA (CCUG 52537) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BAPA_SPHXN] Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar. Publication Abstract from PubMed The beta-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 beta-amino acid residues from peptides. We determined the crystal structures of the native (alphabeta)(4) heterooctamer and of the 153 kDa precursor homotetramer at a resolution of 1.45 and 1.8 A, 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. Autoproteolytic and catalytic mechanisms for the beta-aminopeptidase BapA--a member of the Ntn hydrolase family.,Merz T, Heck T, Geueke B, Mittl PR, Briand C, Seebach D, Kohler HP, Grutter MG Structure. 2012 Nov 7;20(11):1850-60. doi: 10.1016/j.str.2012.07.017. Epub 2012, Sep 12. PMID:22980995 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminopeptidase

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