6A9V
Crystal structure of Icp55 from Saccharomyces cerevisiae (N-terminal 42 residues deletion)
Summary for 6A9V
| Entry DOI | 10.2210/pdb6a9v/pdb |
| Descriptor | Intermediate cleaving peptidase 55, MANGANESE (II) ION, TRIETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | intermediate cleaving peptidase 55, m24b, peptidase, xaa-pro aminopeptidase, mitochondrial, hydrolase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 53358.72 |
| Authors | Singh, R.,Kumar, A.,Goyal, V.D.,Makde, R.D. (deposition date: 2018-07-16, release date: 2019-01-16, Last modification date: 2024-03-27) |
| Primary citation | Singh, R.,Goyal, V.D.,Kumar, A.,Sabharwal, N.S.,Makde, R.D. Crystal structures and biochemical analyses of intermediate cleavage peptidase: role of dynamics in enzymatic function. FEBS Lett., 593:443-454, 2019 Cited by PubMed Abstract: Intermediate cleavage peptidase (Icp55) processes a subset of mitochondrial matrix proteins by removing a bulky residue at their N termini, leaving behind smaller N-terminal residues (icp activity). This contributes towards the stability of the mitochondrial proteome. We report crystal structures of yeast Icp55 including one bound to the apstatin inhibitor. Apart from icp activity, the enzyme was found to exhibit Xaa-Pro aminopeptidase activity in vitro. Structural and biochemical data suggest that the enzyme exists in a rapid equilibrium between monomer and dimer. Furthermore, the dimer, and not the monomer, was found to be the active species with loop dynamics at the dimer interface playing an important role in activity. Based on the new evidence, we propose a model for binding and processing of cellular targets by Icp55. DATABASE: The atomic coordinates and structure factors for the structures of Icp55 (code 6A9T, 6A9U, 6A9V) have been deposited in the Protein Data Bank (PDB) (http://www.pdb.org/). PubMed: 30582634DOI: 10.1002/1873-3468.13321 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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