2pns: Difference between revisions
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New page: left|200px<br /><applet load="2pns" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pns, resolution 1.90Å" /> '''1.9 Angstrom resolut... |
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== | ==1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence== | ||
We report here the cloning and characterization of the entire cDNA of a | <StructureSection load='2pns' size='340' side='right'caption='[[2pns]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2pns]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pns OCA], [https://pdbe.org/2pns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pns RCSB], [https://www.ebi.ac.uk/pdbsum/2pns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pns ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ERVC1_TABDI ERVC1_TABDI] Cysteine proteinase (PubMed:9836431). Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity (PubMed:9836431). Has little or no activity against synthetic substrates (PubMed:9836431).<ref>PMID:9836431</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pn/2pns_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pns ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:17767923</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 2pns" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tabernaemontana divaricata]] | [[Category: Tabernaemontana divaricata]] | ||
[[Category: Biswas | [[Category: Biswas S]] | ||
[[Category: Chakrabarti | [[Category: Chakrabarti C]] | ||
[[Category: Dattagupta | [[Category: Dattagupta JK]] | ||
[[Category: Ghosh | [[Category: Ghosh R]] | ||
[[Category: Thakurta | [[Category: Guha Thakurta P]] | ||
Latest revision as of 09:47, 25 December 2024
1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence
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