4FZG
20S yeast proteasome in complex with glidobactin
Summary for 4FZG
| Entry DOI | 10.2210/pdb4fzg/pdb |
| Related | 1RYP 2CZY 3BDM 4FZC |
| Related PRD ID | PRD_001016 |
| Descriptor | Proteasome component Y7, Proteasome component C11, Proteasome component PRE2, ... (16 entities in total) |
| Functional Keywords | ubiquitin, proteasome, drug development, inhibitor, natural product, n-terminal nucleophilic hydrolase, protein degradation, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 32 |
| Total formula weight | 706369.01 |
| Authors | Stein, M.,Beck, P.,Kaiser, M.,Dudler, R.,Becker, C.F.W.,Groll, M. (deposition date: 2012-07-06, release date: 2012-10-24, Last modification date: 2023-11-15) |
| Primary citation | Stein, M.L.,Beck, P.,Kaiser, M.,Dudler, R.,Becker, C.F.,Groll, M. One-shot NMR analysis of microbial secretions identifies highly potent proteasome inhibitor. Proc.Natl.Acad.Sci.USA, 109:18367-18371, 2012 Cited by PubMed Abstract: Natural products represent valuable lead structures for drug discovery. However, for most bioactive compounds no cellular target is yet identified and many substances predicted from genome analysis are inaccessible due to their life stage-dependent biosynthesis, which is not reflected in common isolation procedures. In response to these issues, an NMR-based and target-directed protease assay for inhibitor detection of the proteasome was developed. The methodology is suitable for one-shot identification of inhibitors in conglomerates and crude culture broths. The technique was applied for analysis of the different life stages of the bacterium Photorhabdus luminescens, which resulted in the isolation and characterization of cepafungin I (CepI), the strongest proteasome inhibitor described to date. Its biosynthesis is strictly regulated and solely induced by the specific environmental conditions determined by our methodology. The transferability of the developed technique to other drug targets may disclose an abundance of novel compounds applicable for drug development. PubMed: 23091006DOI: 10.1073/pnas.1211423109 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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