6QEB
Assessment of a large enzyme-drug complex by proton-detected solid-state NMR without deuteration
Summary for 6QEB
| Entry DOI | 10.2210/pdb6qeb/pdb |
| NMR Information | BMRB: 34347 |
| Descriptor | Carbonic anhydrase 2, ZINC ION, 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE (3 entities in total) |
| Functional Keywords | hcaii solid state nmr acetazolamide, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 29576.72 |
| Authors | Vasa, S.K. (deposition date: 2019-01-07, release date: 2019-02-06, Last modification date: 2024-06-19) |
| Primary citation | Vasa, S.K.,Singh, H.,Grohe, K.,Linser, R. Assessment of a Large Enzyme-Drug Complex by Proton-Detected Solid-State NMR Spectroscopy without Deuteration. Angew.Chem.Int.Ed.Engl., 58:5758-5762, 2019 Cited by PubMed Abstract: Solid-state NMR spectroscopy has recently enabled structural biology with small amounts of non-deuterated proteins, largely alleviating the classical sample production demands. Still, despite the benefits for sample preparation, successful and comprehensive characterization of complex spin systems in the few cases of higher-molecular-weight proteins has thus far relied on traditional C-detected methodology or sample deuteration. Herein we show for a 29 kDa carbonic anhydrase:acetazolamide complex that different aspects of solid-state NMR assessment of a complex spin system can be successfully accessed using a non-deuterated, 500 μg sample in combination with adequate spectroscopic tools. The shown access to protein structure, protein dynamics, as well as biochemical parameters in amino acid sidechains, such as histidine protonation states, will be transferable to proteins that are not expressible in E. coli. PubMed: 30688395DOI: 10.1002/anie.201811714 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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