4e1q: Difference between revisions

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 == Structural highlights ==
 <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='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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.251&#8491;</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>
 </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]
+[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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4e1q" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>