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| | ==Crystal structure of a dimeric cyclophilin A from T.vaginalis== | | ==Crystal structure of a dimeric cyclophilin A from T.vaginalis== |
| - | <StructureSection load='5yb9' size='340' side='right' caption='[[5yb9]], [[Resolution|resolution]] 2.28Å' scene=''> | + | <StructureSection load='5yb9' size='340' side='right'caption='[[5yb9]], [[Resolution|resolution]] 2.28Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yb9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Triva Triva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YB9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YB9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yb9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YB9 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TVAG_004440 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5722 TRIVA])</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]] 2.276Å</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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yb9 OCA], [https://pdbe.org/5yb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yb9 RCSB], [https://www.ebi.ac.uk/pdbsum/5yb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yb9 ProSAT]</span></td></tr> |
| - | <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=5yb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yb9 OCA], [http://pdbe.org/5yb9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yb9 RCSB], [http://www.ebi.ac.uk/pdbsum/5yb9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yb9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A2DT06_TRIVA A2DT06_TRIVA]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU363019] | + | [https://www.uniprot.org/uniprot/A2DT06_TRIV3 A2DT06_TRIV3] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU363019] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Peptidylprolyl isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Triva]] | + | [[Category: Trichomonas vaginalis]] |
| - | [[Category: Chen, C]] | + | [[Category: Chen C]] |
| - | [[Category: Cho, C C]] | + | [[Category: Cho CC]] |
| - | [[Category: Chou, C C]] | + | [[Category: Chou CC]] |
| - | [[Category: Hsu, C H]] | + | [[Category: Hsu CH]] |
| - | [[Category: Lin, M H]] | + | [[Category: Lin MH]] |
| - | [[Category: Martin, T]] | + | [[Category: Martin T]] |
| - | [[Category: Cyclophilin some]]
| + | |
| - | [[Category: Dimeric cyclophilin]]
| + | |
| - | [[Category: Divergent loop cyclophilin]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
A2DT06_TRIV3 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU363019]
Publication Abstract from PubMed
Cyclophilin 1 (TvCyP1), a cyclophilin type peptidyl-prolyl isomerase present in the human parasite Trichomonas vaginalis, interacts with Myb1 and assists in its nuclear translocation. Myb1 regulates the expression of ap65-1 gene that encodes for a disease causing cytoadherence enzyme. Here, we determined the crystal structures of TvCyP1 and its complex with the minimum TvCyP1-binding sequence of Myb1 (Myb1(104-111)), where TvCyP1 formed a homodimer, unlike other single domain cyclophilins. In the complex structure, one Myb1(104-111) peptide was bound to each TvCyP1 protomer, with G106-P107 and Y105 fitting well into the active site and auxiliary S2 pocket, respectively. NMR data further showed that TvCyP1 can catalyze the cis/trans isomerization of P107 in Myb1(104-111). Interestingly, in the well-folded Myb1 protein (Myb1(35-141)), the minimum binding sequence adopted a different conformation from that of unstructured Myb1(104-111) peptide, that could make P107 binding to the active site of TvCyP1 difficult. However, NMR studies showed that similar to Myb1(104-111) peptide, Myb1(35-141) also interacted with the active site of TvCyP1 and the dynamics of the Myb1(35-141) residues near P107 was reduced upon interaction. Together, the structure of TvCyP1 and detailed structural insights on TvCyP1-Myb1 interaction provided here could pave the way for newer drugs to treat drug-resistant strains.
Structural basis of interaction between dimeric cyclophilin 1 and Myb1 transcription factor in Trichomonas vaginalis.,Martin T, Lou YC, Chou CC, Wei SY, Sadotra S, Cho CC, Lin MH, Tai JH, Hsu CH, Chen C Sci Rep. 2018 Apr 3;8(1):5410. doi: 10.1038/s41598-018-23821-5. PMID:29615721[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martin T, Lou YC, Chou CC, Wei SY, Sadotra S, Cho CC, Lin MH, Tai JH, Hsu CH, Chen C. Structural basis of interaction between dimeric cyclophilin 1 and Myb1 transcription factor in Trichomonas vaginalis. Sci Rep. 2018 Apr 3;8(1):5410. doi: 10.1038/s41598-018-23821-5. PMID:29615721 doi:http://dx.doi.org/10.1038/s41598-018-23821-5
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