5LAJ
Ligand-induced Lys33-Thr1 crosslinking at the yeast proteasomal subunit beta5 by sulfonate esters
Summary for 5LAJ
| Entry DOI | 10.2210/pdb5laj/pdb |
| Related | 4R18 5CZ4 |
| Descriptor | Proteasome subunit alpha type-2, Proteasome subunit beta type-4, Proteasome subunit beta type-5, ... (16 entities in total) |
| Functional Keywords | proteasome, fluorescent probes, binding analysis, umpolung, crosslink, hydrolase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 28 |
| Total formula weight | 731318.13 |
| Authors | Groll, M.,Dubiella, C.,Cui, H. (deposition date: 2016-06-14, release date: 2017-04-26, Last modification date: 2024-01-10) |
| Primary citation | Dubiella, C.,Cui, H.,Groll, M. Tunable Probes with Direct Fluorescence Signals for the Constitutive and Immunoproteasome. Angew. Chem. Int. Ed. Engl., 55:13330-13334, 2016 Cited by PubMed Abstract: Electrophiles are commonly used for the inhibition of proteases. Notably, inhibitors of the proteasome, a central determinant of cellular survival and a target of several FDA-approved drugs, are mainly characterized by the reactivity of their electrophilic head groups. We aimed to tune the inhibitory strength of peptidic sulfonate esters by varying the leaving groups. Indeed, proteasome inhibition correlated well with the pK of the leaving group. The use of fluorophores as leaving groups enabled us to design probes that release a stoichiometric fluorescence signal upon reaction, thereby directly linking proteasome inactivation to the readout. This principle could be applicable to other sulfonyl fluoride based inhibitors and allows the design of sensitive probes for enzymatic studies. PubMed: 27709817DOI: 10.1002/anie.201605753 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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