6S8Z

Elongation Factor P from Corynebacterium glutamicum

Summary for 6S8Z

• Entry DOI: 10.2210/pdb6s8z/pdb
• Descriptor: Elongation factor P, ACETATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: elongation factor p, translation
• Biological source: Corynebacterium glutamicum
• Total number of polymer chains: 1
• Total formula weight: 20927.38

Authors

Schneider, S.,Scheidler, C.M. (deposition date: 2019-07-11, release date: 2020-02-26, Last modification date: 2024-01-24)

Primary citation

Pinheiro, B.,Scheidler, C.M.,Kielkowski, P.,Schmid, M.,Forne, I.,Ye, S.,Reiling, N.,Takano, E.,Imhof, A.,Sieber, S.A.,Schneider, S.,Jung, K.
Structure and Function of an Elongation Factor P Subfamily in Actinobacteria.
Cell Rep, 30:4332-4342.e5, 2020

PubMed Abstract: Translation of consecutive proline motifs causes ribosome stalling and requires rescue via the action of a specific translation elongation factor, EF-P in bacteria and archaeal/eukaryotic a/eIF5A. In Eukarya, Archaea, and all bacteria investigated so far, the functionality of this translation elongation factor depends on specific and rather unusual post-translational modifications. The phylum Actinobacteria, which includes the genera Corynebacterium, Mycobacterium, and Streptomyces, is of both medical and economic significance. Here, we report that EF-P is required in these bacteria in particular for the translation of proteins involved in amino acid and secondary metabolite production. Notably, EF-P of Actinobacteria species does not need any post-translational modification for activation. While the function and overall 3D structure of this EF-P type is conserved, the loop containing the conserved lysine is flanked by two essential prolines that rigidify it. Actinobacteria's EF-P represents a unique subfamily that works without any modification.

PubMed: 32234471
DOI: 10.1016/j.celrep.2020.03.009

Experimental method

X-RAY DIFFRACTION (2.2 Å)