3RFY

Crystal structure of arabidopsis thaliana cyclophilin 38 (ATCYP38)

Summary for 3RFY

• Entry DOI: 10.2210/pdb3rfy/pdb
• Descriptor: Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic (2 entities in total)
• Functional Keywords: cyclophilin, cyp38, peptidyl prolyl isomerase, ppiase, tlp, isomerase
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Plastid, chloroplast thylakoid lumen : Q9SSA5
• Total number of polymer chains: 1
• Total formula weight: 40418.68

Authors

Vasudevan, D.,Swaminathan, K. (deposition date: 2011-04-07, release date: 2012-06-13, Last modification date: 2024-03-20)

Primary citation

Vasudevan, D.,Fu, A.,Luan, S.,Swaminathan, K.
Crystal structure of Arabidopsis cyclophilin38 reveals a previously uncharacterized immunophilin fold and a possible autoinhibitory mechanism.
Plant Cell, 24:2666-2674, 2012

PubMed 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.

PubMed: 22706283
DOI: 10.1105/tpc.111.093781

Experimental method

X-RAY DIFFRACTION (2.39 Å)