5NVG
Thr12 Phosphorylated Ubiquitin
Summary for 5NVG
Entry DOI | 10.2210/pdb5nvg/pdb |
Descriptor | Polyubiquitin-B, PHOSPHATE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
Functional Keywords | ubiquitin phosphoubiquitin phosphorylation phosphothreonine, signaling protein |
Biological source | Homo sapiens (Human) |
Cellular location | Ubiquitin: Cytoplasm : P0CG47 |
Total number of polymer chains | 1 |
Total formula weight | 8857.90 |
Authors | Huguenin-Dezot, N. (deposition date: 2017-05-04, release date: 2017-05-31, Last modification date: 2024-10-23) |
Primary citation | Zhang, M.S.,Brunner, S.F.,Huguenin-Dezot, N.,Liang, A.D.,Schmied, W.H.,Rogerson, D.T.,Chin, J.W. Biosynthesis and genetic encoding of phosphothreonine through parallel selection and deep sequencing. Nat. Methods, 14:729-736, 2017 Cited by PubMed Abstract: The phosphorylation of threonine residues in proteins regulates diverse processes in eukaryotic cells, and thousands of threonine phosphorylations have been identified. An understanding of how threonine phosphorylation regulates biological function will be accelerated by general methods to biosynthesize defined phosphoproteins. Here we describe a rapid approach for directly discovering aminoacyl-tRNA synthetase-tRNA pairs that selectively incorporate non-natural amino acids into proteins; our method uses parallel positive selections combined with deep sequencing and statistical analysis and enables the direct, scalable discovery of aminoacyl-tRNA synthetase-tRNA pairs with mutually orthogonal substrate specificity. By combining a method to biosynthesize phosphothreonine in cells with this selection approach, we discover a phosphothreonyl-tRNA synthetase-tRNA pair and create an entirely biosynthetic route to incorporating phosphothreonine in proteins. We biosynthesize several phosphoproteins and demonstrate phosphoprotein structure determination and synthetic protein kinase activation. PubMed: 28553966DOI: 10.1038/nmeth.4302 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.07 Å) |
Structure validation
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