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- Title
Crystal Structure of Arabidopsis Cyclophilin38 Reveals a Previously Uncharacterized Immunophilin Fold and a Possible Autoinhibitory Mechanism.
- Authors
Vasudevan, Dileep; Fu, Aigen; Luan, Sheng; Swaminathan, Kunchithapadam
- 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-Å resolution. The structure reveals two distinct domains: an N-terminal helical bundle and a C-terminal cyclophilin β-barrel, connected by an acidic loop. Two N-terminal β-strands become part of the C-terminal cyclophilin β-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.
- Subjects
ISOMERASES; CRYSTAL structure; PROTEIN-protein interactions; CYCLOPHILINS; ARABIDOPSIS; PROTEIN structure; PROTEIN domains
- Publication
Plant Cell, 2012, Vol 24, Issue 6, p2666
- ISSN
1040-4651
- Publication type
Article
- DOI
10.1105/tpc.111.093781