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PDBsum entry 2pns
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References listed in PDB file
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Key reference
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Title
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A thermostable cysteine protease precursor from a tropical plant contains an unusual c-Terminal propeptide: cdna cloning, Sequence comparison and molecular modeling studies.
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Authors
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R.Ghosh,
J.K.Dattagupta,
S.Biswas.
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Ref.
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Biochem Biophys Res Commun, 2007,
362,
965-970.
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PubMed id
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Abstract
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We report here the cloning and characterization of the entire cDNA of a
papain-like cysteine protease from a tropical flowering plant. The 1098-bp ORF
of the cDNA codify a protease precursor having a signal peptide of 19 amino
acids, a cathepsin-L like N-terminal proregion of 114 amino acids, a mature
enzyme part of 208 amino acids and a C-terminal proregion of 24 amino acids. The
derived amino acid sequence of the mature part tallies with the thermostable
cysteine protease Ervatamin-C--as was aimed at. The C-terminal proregion of the
protease has altogether a different sequence pattern not observed in other
members of the family and it contains a negatively charged helical zone. The
three-dimensional model of the precursor, based on the homology modeling and
X-ray structure, shows that the extended peptide stretch region of the
N-terminal propeptide, covering the interdomain cleft, contains protruding side
chains of positively charged residues. This study also indicates that the
negatively charged zone of C-terminal propeptide may interact with the
positively charged zone of the N-terminal propeptide in a cooperative manner in
the maturation process of this enzyme.
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