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| <StructureSection load='3t1u' size='340' side='right'caption='[[3t1u]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3t1u' size='340' side='right'caption='[[3t1u]], [[Resolution|resolution]] 2.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3t1u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azovd Azovd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T1U FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3t1u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii_DJ Azotobacter vinelandii DJ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T1U FirstGlance]. <br> |
| </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NIT:4-NITROANILINE'>NIT</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></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]] 2Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t17|3t17]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NIT:4-NITROANILINE'>NIT</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Avin_23510 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=322710 AZOVD])</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=3t1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1u OCA], [https://pdbe.org/3t1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t1u RCSB], [https://www.ebi.ac.uk/pdbsum/3t1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1u 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=3t1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1u OCA], [http://pdbe.org/3t1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t1u RCSB], [http://www.ebi.ac.uk/pdbsum/3t1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1u ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/C1DHE4_AZOVD C1DHE4_AZOVD]] PPIases accelerate the folding of proteins. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] | | [https://www.uniprot.org/uniprot/C1DHE4_AZOVD C1DHE4_AZOVD] PPIases accelerate the folding of proteins. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Cyclophilins constitute a class of peptidyl-prolyl isomerases which participate in processes related to protein folding, signalling and chaperoning. The crystal structure of the cytoplasmic cyclophilin A (CyPA) from the bacterium Azotobacter vinelandii complexed with a synthetic tetrapeptide was determined by molecular replacement at 2 resolution. The proline in the tetrapeptide is observed to adopt the cis-isomer conformation. Comparisons of this structure with other CyPA structures provide insights into the conformational variability, effects of peptide binding and structure-function relationships of this enzyme.
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| Structure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptide.,Christoforides E, Dimou M, Katinakis P, Bethanis K, Karpusas M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):259-64., Epub 2012 Feb 15. PMID:22442217<ref>PMID:22442217</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3t1u" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Azovd]] | | [[Category: Azotobacter vinelandii DJ]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Peptidylprolyl isomerase]]
| | [[Category: Bethanis K]] |
| [[Category: Bethanis, K]] | | [[Category: Christoforides E]] |
| [[Category: Christoforides, E]] | | [[Category: Dimou M]] |
| [[Category: Dimou, M]] | | [[Category: Karpusas M]] |
| [[Category: Karpusas, M]] | | [[Category: Katinakis P]] |
| [[Category: Katinakis, P]] | |
| [[Category: Isomerase]]
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| [[Category: Peptidyl-prolyl isomerase]]
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| [[Category: Ppiase]]
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