2PNS

1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence

Summary for 2PNS

• Entry DOI: 10.2210/pdb2pns/pdb
• Related: 1O0E
• Descriptor: Ervatamin-C, a papain-like plant cysteine protease, PHOSPHATE ION, THIOSULFATE, ... (4 entities in total)
• Functional Keywords: papain-like fold, thermostable, plant cysteine protease, ervatamin, hydrolase
• Biological source: Tabernaemontana divaricata
• Cellular location: Secreted: P83654
• Total number of polymer chains: 2
• Total formula weight: 46307.89

Authors

Ghosh, R.,Guha Thakurta, P.,Biswas, S.,Chakrabarti, C.,Dattagupta, J.K. (deposition date: 2007-04-25, release date: 2007-06-19, Last modification date: 2023-08-30)

Primary citation

Ghosh, R.,Dattagupta, J.K.,Biswas, S.
A thermostable cysteine protease precursor from a tropical plant contains an unusual C-terminal propeptide: cDNA cloning, sequence comparison and molecular modeling studies.
Biochem.Biophys.Res.Commun., 362:965-970, 2007

PubMed Abstract: 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.

PubMed: 17767923
DOI: 10.1016/j.bbrc.2007.08.098

Experimental method

X-RAY DIFFRACTION (1.9 Å)