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4hy7
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4hy7 is ON HOLD Authors: Sekhon, S.S., Jeong, D.G., Woo, E.J., Singh, P., Pareek, A., Yoon, T.-S. Description: Structural and biochemical character...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural and biochemical characterization of a cytosolic wheat cyclophilin TaCypA-1== | |
| + | <StructureSection load='4hy7' size='340' side='right'caption='[[4hy7]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hy7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum] and [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HY7 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]] 1.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</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=4hy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hy7 OCA], [https://pdbe.org/4hy7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hy7 RCSB], [https://www.ebi.ac.uk/pdbsum/4hy7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hy7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == 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<ref>PMID:23519664</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4hy7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Tolypocladium inflatum]] | ||
| + | [[Category: Triticum aestivum]] | ||
| + | [[Category: Jeong DG]] | ||
| + | [[Category: Pareek A]] | ||
| + | [[Category: Sekhon SS]] | ||
| + | [[Category: Singh P]] | ||
| + | [[Category: Woo EJ]] | ||
| + | [[Category: Yoon T-S]] | ||
Current revision
Structural and biochemical characterization of a cytosolic wheat cyclophilin TaCypA-1
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