5MI9

Structure of the phosphomimetic mutant of the elongation factor EF-Tu T62E

Summary for 5MI9

• Entry DOI: 10.2210/pdb5mi9/pdb
• Related: 5MI3
• Descriptor: Elongation factor Tu 1, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: phosphomimetic protein, nucleotide binding, conformational cycle, protein dynamics, translation elongation, toxin-antitoxin, hydrolase
• Biological source: Escherichia coli O9:H4 (strain HS)
• Total number of polymer chains: 2
• Total formula weight: 89650.11

Authors

Talavera, A.,Hendrix, J.,Versees, W.,De Gieter, S.,Castro-Roa, D.,Jurenas, D.,Van Nerom, K.,Vandenberk, N.,Barth, A.,De Greve, H.,Hofkens, J.,Zenkin, N.,Loris, R.,Garcia-Pino, A. (deposition date: 2016-11-27, release date: 2017-12-20, Last modification date: 2019-10-16)

• Primary citation: Talavera, A.,Hendrix, J.,Versees, W.,Jurenas, D.,Van Nerom, K.,Vandenberk, N.,Singh, R.K.,Konijnenberg, A.,De Gieter, S.,Castro-Roa, D.,Barth, A.,De Greve, H.,Sobott, F.,Hofkens, J.,Zenkin, N.,Loris, R.,Garcia-Pino, A.; Phosphorylation decelerates conformational dynamics in bacterial translation elongation factors.; Sci Adv, 4:eaap9714-eaap9714, 2018; PubMed: 29546243; DOI: 10.1126/sciadv.aap9714

Experimental method

X-RAY DIFFRACTION (3.3 Å)