|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6hmz' size='340' side='right'caption='[[6hmz]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='6hmz' size='340' side='right'caption='[[6hmz]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hmz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brana Brana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HMZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HMZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hmz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_napus Brassica napus] 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=6HMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HMZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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]] 1.98Å</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> | + | <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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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">BnaA09g35540D, GSBRNA2T00037123001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3708 BRANA])</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=6hmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hmz OCA], [https://pdbe.org/6hmz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hmz RCSB], [https://www.ebi.ac.uk/pdbsum/6hmz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hmz 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=6hmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hmz OCA], [http://pdbe.org/6hmz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hmz RCSB], [http://www.ebi.ac.uk/pdbsum/6hmz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hmz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A078GRH6_BRANA A0A078GRH6_BRANA]] 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/A0A078GRH6_BRANA A0A078GRH6_BRANA] 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 == |
| Line 21: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6hmz" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6hmz" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brana]] | + | [[Category: Brassica napus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidylprolyl isomerase]] | + | [[Category: Tolypocladium inflatum]] |
| - | [[Category: Betzel, C]] | + | [[Category: Betzel C]] |
| - | [[Category: Falke, S]] | + | [[Category: Falke S]] |
| - | [[Category: Garbe, M]] | + | [[Category: Garbe M]] |
| - | [[Category: Hanhart, P]] | + | [[Category: Hanhart P]] |
| - | [[Category: Kehr, J]] | + | [[Category: Kehr J]] |
| - | [[Category: Thiess, M]] | + | [[Category: Thiess M]] |
| - | [[Category: Cyclophilin diversity]]
| + | |
| - | [[Category: Cyclosporin some]]
| + | |
| - | [[Category: Cyp-like domain]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Peptidyl-prolyl cis/trans isomerase]]
| + | |
| - | [[Category: Phloem sap]]
| + | |
| Structural highlights
6hmz is a 2 chain structure with sequence from Brassica napus and Tolypocladium inflatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.98Å |
| Ligands: | , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A0A078GRH6_BRANA 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
Cyclophilins (CYPs) are a group of ubiquitous prolyl cis/trans isomerases (PPIases). It was shown that plants possess the most diverse CYP families and that these are abundant in the phloem long-distance translocation stream. Since phloem exudate showed PPIase activity, three single-domain CYPs that occur in phloem samples from Brassica napus were characterised on functional and structural levels. It could be shown that they exhibit isomerase activity and that this activity is controlled by a redox regulation mechanism, which has been postulated for divergent CYPs. The structure determination by small-angle X-ray scattering experiments revealed a conserved globular shape. In addition, the high-resolution crystal structure of BnCYP19-1 was resolved and refined to 2.0 A resolution, and the active sites of related CYPs as well as substrate binding were modelled. The obtained data and results support the hypothesis that single domain phloem CYPs are active phloem PPIases that may function as chaperones.
Enzyme activity and structural features of three single-domain phloem cyclophilins from Brassica napus.,Hanhart P, Falke S, Garbe M, Rose V, Thiess M, Betzel C, Kehr J Sci Rep. 2019 Jun 27;9(1):9368. doi: 10.1038/s41598-019-45856-y. PMID:31249367[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hanhart P, Falke S, Garbe M, Rose V, Thiess M, Betzel C, Kehr J. Enzyme activity and structural features of three single-domain phloem cyclophilins from Brassica napus. Sci Rep. 2019 Jun 27;9(1):9368. doi: 10.1038/s41598-019-45856-y. PMID:31249367 doi:http://dx.doi.org/10.1038/s41598-019-45856-y
|
