1DG1

WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).

Summary for 1DG1

• Entry DOI: 10.2210/pdb1dg1/pdb
• Related: 1AIP 1B23 1D2E 1DAR 1EFC 1EFM
• Descriptor: ELONGATION FACTOR TU, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: elongation factor, trna binding, alpha beta shift, ts binding protein, gtpase, gdp binding, rna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 87676.00

Authors

Abel, K.,Yoder, M.,Hilgenfeld, R.,Jurnak, F. (deposition date: 1999-11-22, release date: 1999-12-01, Last modification date: 2024-02-07)

Primary citation

Abel, K.,Yoder, M.D.,Hilgenfeld, R.,Jurnak, F.
An alpha to beta conformational switch in EF-Tu.
Structure, 4:1153-1159, 1996

PubMed Abstract: The bacterial elongation factor EF-Tu recognizes and transports aminoacyl-tRNAs to mRNA-programmed ribosomes. EF-Tu shares many structural and functional properties with other GTPases whose conformations are regulated by guanine nucleotides.

PubMed: 8939740
DOI: 10.1016/S0969-2126(96)00123-2

Experimental method

X-RAY DIFFRACTION (2.5 Å)