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PDBsum entry 2k1g
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References listed in PDB file
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Key reference
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Title
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Solution nmr structure of the nlpc/p60 domain of lipoprotein spr from escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad.
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Authors
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J.M.Aramini,
P.Rossi,
Y.J.Huang,
L.Zhao,
M.Jiang,
M.Maglaqui,
R.Xiao,
J.Locke,
R.Nair,
B.Rost,
T.B.Acton,
M.Inouye,
G.T.Montelione.
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Ref.
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Biochemistry, 2008,
47,
9715-9717.
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PubMed id
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Abstract
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Escherichia coli Spr is a membrane-anchored cell wall hydrolase. The solution
NMR structure of the C-terminal NlpC/P60 domain of E. coli Spr described here
reveals that the protein adopts a papain-like alpha+beta fold and identifies a
substrate-binding cleft featuring several highly conserved residues. The active
site features a novel Cys-His-His catalytic triad that appears to be a unique
structural signature of this cysteine peptidase family. Moreover, the relative
orientation of these catalytic residues is similar to that observed in the
analogous Ser-His-His triad, a variant of the classic Ser-His-Asp charge relay
system, suggesting the convergent evolution of a catalytic mechanism in quite
distinct peptidase families.
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