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PDBsum entry 3n33
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Hydrolase/hydrolase inhibitor
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PDB id
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3n33
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References listed in PDB file
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Key reference
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Title
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Autoproteolytic and catalytic mechanisms for the β-Aminopeptidase bapa--A member of the ntn hydrolase family.
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Authors
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T.Merz,
T.Heck,
B.Geueke,
P.R.Mittl,
C.Briand,
D.Seebach,
H.P.Kohler,
M.G.Grütter.
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Ref.
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Structure, 2012,
20,
1850-1860.
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PubMed id
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Abstract
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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.
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