5MI9

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

Summary for 5MI9

Related5MI3
DescriptorElongation factor Tu 1, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordsphosphomimetic protein, nucleotide binding, conformational cycle, protein dynamics, translation elongation, toxin-antitoxin, hydrolase
Biological sourceEscherichia coli O9:H4 (strain HS)
Total number of polymer chains2
Total molecular weight89650.11
Authors
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 (PDB entries with the same primary citation)
DOI: 10.1126/sciadv.aap9714
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (3.3 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.28980 2.9% 1.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution