3DY4
Crystal structure of yeast 20S proteasome in complex with spirolactacystin
Summary for 3DY4
| Entry DOI | 10.2210/pdb3dy4/pdb |
| Related | 1RYP 3DY3 |
| Descriptor | Proteasome component Y7, Proteasome component C11, Proteasome component PRE2, ... (16 entities in total) |
| Functional Keywords | proteasome, inhibitor, protein degradation, ubiquitin-proteasome-pathway, hydrolase, nucleus, protease, threonine protease, phosphoprotein, zymogen |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Cytoplasm: P23639 P22141 P30656 P23724 P30657 P38624 P23638 P40303 P32379 P40302 P21242 P21243 P25043 P25451 |
| Total number of polymer chains | 28 |
| Total formula weight | 705067.22 |
| Authors | Groll, M.,Balskus, E.,Jacobsen, E. (deposition date: 2008-07-25, release date: 2008-11-04, Last modification date: 2024-10-30) |
| Primary citation | Groll, M.,Balskus, E.P.,Jacobsen, E.N. Structural analysis of spiro beta-lactone proteasome inhibitors. J.Am.Chem.Soc., 130:14981-14983, 2008 Cited by PubMed Abstract: Spiro beta-lactone-based proteasome inhibitors were discovered in the context of an asymmetric catalytic total synthesis of the natural product (+)-lactacystin (1). Lactone 4 was found to be a potent inhibitor of the 26S proteasome, while its C-6 epimer (5) displayed weak activity. Crystallographic studies of the two analogues covalently bound to the 20S proteasome permitted characterization of the important stabilizing interactions between each inhibitor and the proteasome's key catalytic N-terminal threonine residue. This structural data support the hypothesis that the discrepancy in potency between 4 and 5 may be due to differences in the hydrolytic stabilities of the resulting acyl enzyme complexes. PubMed: 18928262DOI: 10.1021/ja806059t PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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