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3rfy

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==Crystal structure of arabidopsis thaliana cyclophilin 38 (ATCYP38)==
==Crystal structure of arabidopsis thaliana cyclophilin 38 (ATCYP38)==
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<StructureSection load='3rfy' size='340' side='right' caption='[[3rfy]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
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<StructureSection load='3rfy' size='340' side='right'caption='[[3rfy]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rfy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RFY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rfy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RFY FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At3g01480, CYP38, F4P13.3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.39&#8491;</td></tr>
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<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'>[https://proteopedia.org/fgij/fg.htm?mol=3rfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rfy OCA], [https://pdbe.org/3rfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rfy RCSB], [https://www.ebi.ac.uk/pdbsum/3rfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rfy ProSAT]</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=3rfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rfy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rfy RCSB], [http://www.ebi.ac.uk/pdbsum/3rfy PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CYP38_ARATH CYP38_ARATH] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Required for the assembly and stabilization of PSII.<ref>PMID:17909185</ref>
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Cyclophilin38 (CYP38) is one of the highly divergent cyclophilins from Arabidopsis thaliana. Here, we report the crystal structure of the At-CYP38 protein (residues 83 to 437 of 437 amino acids) at 2.39-A resolution. The structure reveals two distinct domains: an N-terminal helical bundle and a C-terminal cyclophilin beta-barrel, connected by an acidic loop. Two N-terminal beta-strands become part of the C-terminal cyclophilin beta-barrel, thereby making a previously undiscovered domain organization. This study shows that CYP38 does not possess peptidyl-prolyl cis/trans isomerase activity and identifies a possible interaction of CYP38 with the E-loop of chlorophyll protein47 (CP47), a component of photosystem II. The interaction of CYP38 with the E-loop of CP47 is mediated through its cyclophilin domain. The N-terminal helical domain is closely packed together with the putative C-terminal cyclophilin domain and establishes a strong intramolecular interaction, thereby preventing the access of the cyclophilin domain to other proteins. This was further verified by protein-protein interaction assays using the yeast two-hybrid system. Furthermore, the non-Leucine zipper N-terminal helical bundle contains several new elements for protein-protein interaction that may be of functional significance. Together, this study provides the structure of a plant cyclophilin and explains a possible mechanism for autoinhibition of its function through an intramolecular interaction.
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Crystal structure of Arabidopsis cyclophilin38 reveals a previously uncharacterized immunophilin fold and a possible autoinhibitory mechanism.,Vasudevan D, Fu A, Luan S, Swaminathan K Plant Cell. 2012 Jun;24(6):2666-74. doi: 10.1105/tpc.111.093781. Epub 2012 Jun, 15. PMID:22706283<ref>PMID:22706283</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Swaminathan, K]]
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[[Category: Swaminathan K]]
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[[Category: Vasudevan, D]]
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[[Category: Vasudevan D]]
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[[Category: Cyclophilin]]
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[[Category: Cyp38]]
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[[Category: Isomerase]]
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[[Category: Peptidyl prolyl isomerase]]
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[[Category: Ppiase]]
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[[Category: Tlp]]
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Current revision

Crystal structure of arabidopsis thaliana cyclophilin 38 (ATCYP38)

PDB ID 3rfy

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