4PHG
Crystal structure of Ypt7 covalently modified with GTP
Summary for 4PHG
| Entry DOI | 10.2210/pdb4phg/pdb |
| Related | 4PHF 4PHH |
| Descriptor | GTP-binding protein YPT7, MAGNESIUM ION, N-[3-(propanoylamino)propyl]guanosine 5'-(tetrahydrogen triphosphate), ... (5 entities in total) |
| Functional Keywords | ypt7, acryl-nucleotides, agtp, covalent, endocytosis, exocytosis |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 21226.34 |
| Authors | Koch, D.,Wiegandt, D.,Vieweg, S.,Hofmann, F.,Wu, Y.,Itzen, A.,Mueller, M.P.,Goody, R.S. (deposition date: 2014-05-06, release date: 2014-05-28, Last modification date: 2024-10-16) |
| Primary citation | Wiegandt, D.,Vieweg, S.,Hofmann, F.,Koch, D.,Li, F.,Wu, Y.W.,Itzen, A.,Muller, M.P.,Goody, R.S. Locking GTPases covalently in their functional states. Nat Commun, 6:7773-7773, 2015 Cited by PubMed Abstract: GTPases act as key regulators of many cellular processes by switching between active (GTP-bound) and inactive (GDP-bound) states. In many cases, understanding their mode of action has been aided by artificially stabilizing one of these states either by designing mutant proteins or by complexation with non-hydrolysable GTP analogues. Because of inherent disadvantages in these approaches, we have developed acryl-bearing GTP and GDP derivatives that can be covalently linked with strategically placed cysteines within the GTPase of interest. Binding studies with GTPase-interacting proteins and X-ray crystallography analysis demonstrate that the molecular properties of the covalent GTPase-acryl-nucleotide adducts are a faithful reflection of those of the corresponding native states and are advantageously permanently locked in a defined nucleotide (that is active or inactive) state. In a first application, in vivo experiments using covalently locked Rab5 variants provide new insights into the mechanism of correct intracellular localization of Rab proteins. PubMed: 26178622DOI: 10.1038/ncomms8773 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
