2pns
From Proteopedia
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- | [[Image:2pns.jpg|left|200px]] | + | [[Image:2pns.jpg|left|200px]] |
- | + | ||
- | '''1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence''' | + | {{Structure |
+ | |PDB= 2pns |SIZE=350|CAPTION= <scene name='initialview01'>2pns</scene>, resolution 1.90Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=THJ:TETRATHIONATE'>THJ</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2PNS is a [ | + | 2PNS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17767923 17767923] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Tabernaemontana divaricata]] | [[Category: Tabernaemontana divaricata]] | ||
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[[Category: thermostable]] | [[Category: thermostable]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:15:20 2008'' |
Revision as of 16:15, 20 March 2008
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, resolution 1.90Å | |||||||
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Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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