Journal
PROTEIN SCIENCE
Volume 20, Issue 3, Pages 630-639Publisher
WILEY-BLACKWELL
DOI: 10.1002/pro.584
Keywords
conformational switch; solid state NMR; conformational selection model; deubiquitinating enzyme; crystal contact
Categories
Funding
- NSF [MCB 0316248]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0749381] Funding Source: National Science Foundation
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A new crystal structure of human ubiquitin is reported at 1.8 angstrom resolution. Compared with the other known crystal structure or the solution NMR structure of monomeric human ubiquitin, this new structure is similar in its overall fold but differs with respect to the conformation of the backbone in a surface-exposed region. The conformation reported here resembles conformations previously seen in complex with deubiquinating enzymes, wherein the Asp52/Gly53 main chain and Glu24 side chain move. This movement exposes the backbone carbonyl of Asp52 to the exterior of the molecule, making it possible to engage in hydrogen-bond contacts with neighboring molecules, rather than in an internal hydrogen bond with the backbone of Glu24. This particular crystal form of ubiquitin has been used in a large number of solid state NMR studies. The structure described here elucidates the origin of many of the chemical shift differences comparing solution and solid state studies.
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