2pns
From Proteopedia
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1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence
Overview
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.
About this Structure
2PNS is a Protein complex structure of sequences from Tabernaemontana divaricata with and as ligands. Full crystallographic information is available from OCA.
Reference
A thermostable cysteine protease precursor from a tropical plant contains an unusual C-terminal propeptide: cDNA cloning, sequence comparison and molecular modeling studies., Ghosh R, Dattagupta JK, Biswas S, Biochem Biophys Res Commun. 2007 Nov 3;362(4):965-70. Epub 2007 Aug 28. PMID:17767923
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