2BV3

Crystal structure of a mutant elongation factor G trapped with a GTP analogue

Summary for 2BV3

• Entry DOI: 10.2210/pdb2bv3/pdb
• Related: 1DAR 1EFG 1ELO 1FNM 1IP8 1IPM 1IPO 1IPR 1JQM 1JQS 1KTV 1PN6 2BM0 2BM1 2EFG
• Descriptor: ELONGATION FACTOR G, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: switch ii, elongation factor, gtp-binding, translation mutation thr84ala, protein biosynthesis
• Biological source: THERMUS THERMOPHILUS
• Cellular location: Cytoplasm: P13551
• Total number of polymer chains: 1
• Total formula weight: 77303.34

Authors

Hansson, S.,Singh, R.,Gudkov, A.T.,Liljas, A.,Logan, D.T. (deposition date: 2005-06-22, release date: 2005-08-10, Last modification date: 2023-12-13)

Primary citation

Hansson, S.,Singh, R.,Gudkov, A.T.,Liljas, A.,Logan, D.T.
Crystal Structure of a Mutant Elongation Factor G Trapped with a GTP Analogue.
FEBS Lett., 579:4492-, 2005

PubMed Abstract: Elongation factor G (EF-G) is a G protein factor that catalyzes the translocation step in protein synthesis on the ribosome. Its GTP conformation in the absence of the ribosome is currently unknown. We present the structure of a mutant EF-G (T84A) in complex with the non-hydrolysable GTP analogue GDPNP. The crystal structure provides a first insight into conformational changes induced in EF-G by GTP. Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome.

PubMed: 16083884
DOI: 10.1016/J.FEBSLET.2005.07.016

Experimental method

X-RAY DIFFRACTION (2.5 Å)