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| | ==Crystal structure of Wheat Cyclophilin A at 1.25 A resolution== | | ==Crystal structure of Wheat Cyclophilin A at 1.25 A resolution== |
| - | <StructureSection load='4e1q' size='340' side='right' caption='[[4e1q]], [[Resolution|resolution]] 1.25Å' scene=''> | + | <StructureSection load='4e1q' size='340' side='right'caption='[[4e1q]], [[Resolution|resolution]] 1.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4e1q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canadian_hard_winter_wheat Canadian hard winter wheat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E1Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4e1q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1Q FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CyP3, CyP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4565 Canadian hard winter wheat])</td></tr> | + | </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=4e1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1q OCA], [https://pdbe.org/4e1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1q RCSB], [https://www.ebi.ac.uk/pdbsum/4e1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1q ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1q OCA], [http://pdbe.org/4e1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e1q RCSB], [http://www.ebi.ac.uk/pdbsum/4e1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q93W25_WHEAT Q93W25_WHEAT]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223] | + | [[https://www.uniprot.org/uniprot/Q93W25_WHEAT Q93W25_WHEAT]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Cyclophilin|Cyclophilin]] | + | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Canadian hard winter wheat]] | + | [[Category: Large Structures]] |
| - | [[Category: Peptidylprolyl isomerase]] | + | [[Category: Triticum aestivum]] |
| - | [[Category: Jeong, D G]] | + | [[Category: Jeong DG]] |
| - | [[Category: Sekhon, S S]] | + | [[Category: Sekhon SS]] |
| - | [[Category: Singh, P]] | + | [[Category: Singh P]] |
| - | [[Category: Woo, E J]] | + | [[Category: Woo EJ]] |
| - | [[Category: Yoon, T S]] | + | [[Category: Yoon TS]] |
| - | [[Category: Isomerase]]
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| Structural highlights
Function
[Q93W25_WHEAT] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223]
Publication Abstract from PubMed
Cyclophilins belong to a family of proteins that bind to the immunosuppressive drug cyclosporin A (CsA). Several members of this protein family catalyze the cis-trans isomerization of peptide bonds preceding prolyl residues. The present study describes the biochemical and structural characteristics of a cytosolic cyclophilin (TaCypA-1) cloned from wheat (Triticum aestivum L.). Purified TaCypA-1 expressed in Escherichia coli showed peptidyl-prolyl cis-trans isomerase activity, which was inhibited by CsA with an inhibition constant of 78.3 nM. The specific activity and catalytic efficiency (kcat/Km) of the purified TaCypA-1 were 99.06 +/- 0.13 nmol s(-1) mg(-1) and 2.32 x 10(5) M(-1) s(-1), respectively. The structures of apo TaCypA-1 and the TaCypA-1-CsA complex were determined at 1.25 and 1.20 A resolution, respectively, using X-ray diffraction. Binding of CsA to the active site of TaCypA-1 did not result in any significant conformational change in the apo TaCypA-1 structure. This is consistent with the crystal structure of the human cyclophilin D-CsA complex reported at 0.96 A resolution. The TaCypA-1 structure revealed the presence of a divergent loop of seven amino acids (48)KSGKPLH(54) which is a characteristic feature of plant cyclophilins. This study is the first to elucidate the structure of an enzymatically active plant cyclophilin which shows peptidyl-prolyl cis-trans isomerase activity and the presence of a divergent loop.
Structural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1.,Sekhon SS, Kaur H, Dutta T, Singh K, Kumari S, Kang S, Park SG, Park BC, Jeong DG, Pareek A, Woo EJ, Singh P, Yoon TS Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):555-63. doi:, 10.1107/S0907444912051529. Epub 2013 Mar 9. PMID:23519664[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sekhon SS, Kaur H, Dutta T, Singh K, Kumari S, Kang S, Park SG, Park BC, Jeong DG, Pareek A, Woo EJ, Singh P, Yoon TS. Structural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1. Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):555-63. doi:, 10.1107/S0907444912051529. Epub 2013 Mar 9. PMID:23519664 doi:10.1107/S0907444912051529
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