9F8W
Crystal structure of the apo Pex5 peroxisomal cargo receptor from Trypanosoma brucei
Summary for 9F8W
| Entry DOI | 10.2210/pdb9f8w/pdb |
| Descriptor | Peroxisome targeting signal 1 receptor PEX5 (2 entities in total) |
| Functional Keywords | trypanosoma, peroxin, peroxin targeting signal, peptide binding protein |
| Biological source | Trypanosoma brucei |
| Total number of polymer chains | 2 |
| Total formula weight | 77839.02 |
| Authors | Banasik, M.K.,Dubin, G. (deposition date: 2024-05-07, release date: 2024-10-02, Last modification date: 2024-10-16) |
| Primary citation | Banasik, M.,Napolitano, V.,Blat, A.,Abdulkarim, K.,Plewka, J.,Czaplewski, C.,Gieldon, A.,Kozak, M.,Wladyka, B.,Popowicz, G.,Dubin, G. Structural dynamics of the TPR domain of the peroxisomal cargo receptor Pex5 in Trypanosoma. Int.J.Biol.Macromol., 280:135510-135510, 2024 Cited by PubMed Abstract: Peroxisomal protein import has been identified as a valid target in trypanosomiases, an important health threat in Central and South America. The importomer is built of multiple peroxins (Pex) and structural characterization of these proteins facilitates rational inhibitor development. We report crystal structures of the Trypanosoma brucei and T. cruzi tetratricopeptide repeat domain (TPR) of the cytoplasmic peroxisomal targeting signal 1 (PTS1) receptor Pex5. The structure of the TPR domain of TbPex5 represents an apo-form of the receptor which, together with the previously determined structure of the complex of TbPex5 TPR and PTS1 demonstrate significant receptor dynamics associated with signal peptide recognition. The structure of the complex of TPR domain of TcPex5 with PTS1 provided in this study details the molecular interactions that guide signal peptide recognition at the atomic level in the pathogenic species currently perceived as the most relevant among Trypanosoma. Small - angle X - ray scattering (SAXS) data obtained in solution supports the crystallographic findings on the compaction of the TPR domains of TbPex5 and TcPex5 upon interaction with the cargo. PubMed: 39304044DOI: 10.1016/j.ijbiomac.2024.135510 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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