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PDBsum entry 1pek
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Hydrolase/hydrolase inhibitor
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PDB id
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1pek
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of the complex of proteinase k with a substrate analogue hexapeptide inhibitor at 2.2-A resolution.
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Authors
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C.Betzel,
T.P.Singh,
M.Visanji,
K.Peters,
S.Fittkau,
W.Saenger,
K.S.Wilson.
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Ref.
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J Biol Chem, 1993,
268,
15854-15858.
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PubMed id
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Abstract
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The crystal structure of a transition state/product complex formed by the
interaction between proteinase K and the substrate analogue
N-Ac-L-Pro-L-Ala-L-Pro-L-Phe-D-Ala-L-Ala-NH2 has been determined at a resolution
of 2.2 A and refined to an R-factor of 0.165 for 12,725 reflections. The
inhibitor forms a stable complex through a series of hydrogen bonds with protein
atoms and water molecules. The inhibitor is hydrolyzed between Phe 4I and
D-Ala5I (I indicates inhibitor). The two fragments are separated by a distance
of 3.07 A between the carbonyl carbon and the main chain nitrogen. Both
fragments remain bound to the protein. The N-terminal fragment occupies subsites
S5 to S1, whereas the C-terminal part is bound in S1' and S2', the first time
that electron density for a substrate analogue has been observed in the P1' and
P2' sites of a subtilisin-like enzyme. The flexible segments of the substrate
recognition sites Gly100-Tyr104 and Ser132-Gly136 move appreciably to
accommodate the inhibitor. Biochemical results indicate an inhibition by this
specifically designed peptide of 95%.
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Secondary reference #1
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Title
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Three-Dimensional structure of proteinase k at 0.15-Nm resolution.
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Authors
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C.Betzel,
G.P.Pal,
W.Saenger.
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Ref.
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Eur J Biochem, 1988,
178,
155-171.
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PubMed id
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