2FBN
Plasmodium falciparum putative FK506-binding protein PFL2275c, C-terminal TPR-containing domain
Summary for 2FBN
| Entry DOI | 10.2210/pdb2fbn/pdb |
| Descriptor | 70 kDa peptidylprolyl isomerase, putative (2 entities in total) |
| Functional Keywords | sulfur sad, pfl2275c, tpr-containing domain, structural genomics, structural genomics consortium, sgc, unknown function |
| Biological source | Plasmodium falciparum (malaria parasite P. falciparum) |
| Total number of polymer chains | 2 |
| Total formula weight | 46075.99 |
| Authors | Dong, A.,Lew, J.,Koeieradzki, I.,Sundararajan, E.,Melone, M.,Wasney, G.,Zhao, Y.,Edwards, A.M.,Arrowsmith, C.H.,Weigelt, J.,Sundstrom, M.,Bochkarev, A.,Hui, R.,Hills, T.,Structural Genomics Consortium (SGC) (deposition date: 2005-12-09, release date: 2006-01-24, Last modification date: 2024-02-14) |
| Primary citation | Alag, R.,Bharatham, N.,Dong, A.,Hills, T.,Harikishore, A.,Widjaja, A.A.,Shochat, S.G.,Hui, R.,Yoon, H.S. Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide. Protein Sci., 18:2115-2124, 2009 Cited by PubMed Abstract: Plasmodium falciparum FK506-binding protein 35 (PfFKBP35) that binds to FK506 contains a conserved tetratricopeptide repeat (TPR) domain. Several known TPR domains such as Hop, PPP5, CHIP, and FKBP52 are structurally conserved and are able to interact with molecular chaperones such as Hsp70/Hsp90. Here, we present the crystal structure of PfFKBP35-TPR and demonstrate its interaction with Hsp90 C-terminal pentapeptide (MEEVD) by surface plasmon resonance and nuclear magnetic resonance spectroscopy-based binding studies. Our sequence and structural analyses reveal that PfFKBP35 is similar to Hop and PPP5 in possessing all the conserved residues which are important for carboxylate clamping with Hsp90. Mutational studies were carried out on positively charged clamp residues that are crucial for binding to carboxylate groups of aspartate, showing that all the mutated residues are important for Hsp90 binding. Molecular docking and electrostatic calculations demonstrated that the MEEVD peptide of Hsp90 can form aspartate clamp unlike FKBP52. Our results provide insightful information and structural basis about the molecular interaction between PfFKBP35-TPR and Hsp90. PubMed: 19691130DOI: 10.1002/pro.226 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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