Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5MI3

Structure of phosphorylated translation elongation factor EF-Tu from E. coli

Summary for 5MI3
Entry DOI10.2210/pdb5mi3/pdb
DescriptorElongation factor Tu 1, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordstranslation elongation, ef-tu, phosphorylation, nucleotide binding, protein dynamics, conformational cycle, toxin-antitoxin, toxin, hydrolase
Biological sourceEscherichia coli (strain K12)
Total number of polymer chains2
Total formula weight89721.91
Authors
Primary citationTalavera, 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
Cited by
PubMed: 29546243
DOI: 10.1126/sciadv.aap9714
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon