3RFY: Crystal structure of arabidopsis thaliana cyclophilin 38 (ATCYP38)

Citation:
Abstract
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.
PDB ID: 3RFYDownload
MMDB ID: 100432
PDB Deposition Date: 2011/4/7
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.39  Å
Source Organism:
Similar Structures:
Biological Unit for 3RFY: monomeric; determined by author
Molecular Components in 3RFY
Label Count Molecule
Protein (1 molecule)
1
Peptidyl-prolyl Cis-trans Isomerase Cyp38, Chloroplastic(Gene symbol: CYP38)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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