2pns

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[[Image:2pns.jpg|left|200px]]<br /><applet load="2pns" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2pns.jpg|left|200px]]
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caption="2pns, resolution 1.90&Aring;" />
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'''1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence'''<br />
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{{Structure
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|PDB= 2pns |SIZE=350|CAPTION= <scene name='initialview01'>2pns</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=THJ:TETRATHIONATE'>THJ</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2PNS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=THJ:'>THJ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNS OCA].
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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==
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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., Ghosh R, Dattagupta JK, Biswas S, Biochem Biophys Res Commun. 2007 Nov 3;362(4):965-70. Epub 2007 Aug 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17767923 17767923]
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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., 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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:23 2008''
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''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


PDB ID 2pns

Drag the structure with the mouse to rotate
, resolution 1.90Å
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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