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PDBsum entry 3csk
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References listed in PDB file
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Key reference
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Title
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The first structure of dipeptidyl-Peptidase III provides insight into the catalytic mechanism and mode of substrate binding.
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Authors
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P.K.Baral,
N.Jajcanin-Jozić,
S.Deller,
P.Macheroux,
M.Abramić,
K.Gruber.
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Ref.
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J Biol Chem, 2008,
283,
22316-22324.
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PubMed id
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Abstract
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Dipeptidyl-peptidases III (DPP III) are zinc-dependent enzymes that specifically
cleave the first two amino acids from the N terminus of different length
peptides. In mammals, DPP III is associated with important physiological
functions and is a potential biomarker for certain types of cancer. Here, we
present the 1.95-A crystal structure of yeast DPP III representing the prototype
for the M49 family of metallopeptidases. It shows a novel fold with two domains
forming a wide cleft containing the catalytic metal ion. DPP III exhibits no
overall similarity to other metallopeptidases, such as thermolysin and
neprilysin, but zinc coordination and catalytically important residues are
structurally conserved. Substrate recognition is accomplished by a binding site
for the N terminus of the peptide at an appropriate distance from the metal
center and by a series of conserved arginine residues anchoring the C termini of
different length substrates.
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