|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of a cyclophilin from Citrus sinensis (CsCyp) in complex with cyclosporin A== | | ==Structure of a cyclophilin from Citrus sinensis (CsCyp) in complex with cyclosporin A== |
| - | <StructureSection load='4jjm' size='340' side='right' caption='[[4jjm]], [[Resolution|resolution]] 2.09Å' scene=''> | + | <StructureSection load='4jjm' size='340' side='right'caption='[[4jjm]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jjm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Citsi Citsi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JJM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jjm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrus_sinensis Citrus sinensis] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JJM FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2711 CITSI])</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=4jjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jjm OCA], [https://pdbe.org/4jjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jjm RCSB], [https://www.ebi.ac.uk/pdbsum/4jjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jjm 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>
| + | |
| - | <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=4jjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jjm OCA], [http://pdbe.org/4jjm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jjm RCSB], [http://www.ebi.ac.uk/pdbsum/4jjm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jjm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/D0ELH5_CITSI D0ELH5_CITSI]] 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/D0ELH5_CITSI D0ELH5_CITSI] 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Citsi]] | + | [[Category: Citrus sinensis]] |
| - | [[Category: Peptidylprolyl isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Ambrosio, A L.B]] | + | [[Category: Tolypocladium inflatum]] |
| - | [[Category: Barbosa, J A.R G]] | + | [[Category: Ambrosio ALB]] |
| - | [[Category: Benedetti, C E]] | + | [[Category: Barbosa JARG]] |
| - | [[Category: Campos, B M]] | + | [[Category: Benedetti CE]] |
| - | [[Category: Souza, T A.C B]] | + | [[Category: Campos BM]] |
| - | [[Category: Cyclophilin]] | + | [[Category: Souza TACB]] |
| - | [[Category: Isomerase-immunosuppressant complex]]
| + | |
| Structural highlights
4jjm is a 4 chain structure with sequence from Citrus sinensis and Tolypocladium inflatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
D0ELH5_CITSI PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]
Publication Abstract from PubMed
The Citrus sinensis cyclophilin CsCyp is a target of the Xanthomonas citri TAL effector PthA, required to elicit cankers on citrus. CsCyp binds the citrus thioredoxin CsTdx and C-terminal domain of RNA Polymerase II (CTD), and is a divergent cyclophilin that carries the additional loop KSGKPLH, invariable cysteines C40 and C168, and conserved glutamate E83. Despite the suggested roles in ATP and metal binding, the function of these unique structural elements remains unknown. Here we show that the conserved cysteines form a disulfide bond that inactivates the enzyme, whereas E83, which belongs to the catalytic loop and is also critical for enzyme activity, is anchored to the divergent loop to maintain the active site open. In addition, we demonstrate that C40 and C168 are required for the interaction with CsTdx and that CsCyp binds the citrus CTD YSPSAP repeat. Our data support the model where formation of the C40-C168 disulfide bond induces a conformational change that disrupts the interaction of the divergent and catalytic loops, via E83, causing the active site to close. This suggests a new type of allosteric regulation in divergent cyclophilins, involving disulfide bond formation and a loop displacement mechanism.
A Redox 2-Cys Mechanism Regulates the Catalytic Activity of Divergent Cyclophilins.,Campos BM, Sforca ML, Ambrosio AL, Domingues MN, Souza TA, Barbosa JA, Leme AF, Perez CA, Whittaker SB, Murakami MT, Zeri AC, Benedetti CE Plant Physiol. 2013 May 24. PMID:23709667[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Campos BM, Sforca ML, Ambrosio AL, Domingues MN, Souza TA, Barbosa JA, Leme AF, Perez CA, Whittaker SB, Murakami MT, Zeri AC, Benedetti CE. A Redox 2-Cys Mechanism Regulates the Catalytic Activity of Divergent Cyclophilins. Plant Physiol. 2013 May 24. PMID:23709667 doi:10.1104/pp.113.218339
|
