Structural highlights
Function
[RIMK_ECOLI] Responsible for the addition of glutamate residues to the C-terminus of ribosomal protein S6.
Publication Abstract from PubMed
Bacterial RimK is an enzyme that catalyzes the polyglutamylation of the C-terminus of ribosomal protein S6 and the synthesis of poly-alpha-L-glutamate peptides using L-glutamic acid. In the present study, the crystal structure of the Escherichia coli RimK protein complexed with the ATP analogue AMP-PNP was determined at 2.05 A resolution. Two different conformations of RimK, closed and open forms, were observed in the crystals. The structural polymorphism revealed in this study provided important information to understand the mechanism by which RimK catalyzes the synthesis of poly-alpha-L-glutamate peptides and the polyglutamylation of ribosomal protein S6.
Structural polymorphism of the Escherichia coli poly-alpha-L-glutamate synthetase RimK.,Arimura Y, Kono T, Kino K, Kurumizaka H Acta Crystallogr F Struct Biol Commun. 2018 Jul 1;74(Pt 7):385-390. doi:, 10.1107/S2053230X18007689. Epub 2018 Jun 26. PMID:29969101[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arimura Y, Kono T, Kino K, Kurumizaka H. Structural polymorphism of the Escherichia coli poly-alpha-L-glutamate synthetase RimK. Acta Crystallogr F Struct Biol Commun. 2018 Jul 1;74(Pt 7):385-390. doi:, 10.1107/S2053230X18007689. Epub 2018 Jun 26. PMID:29969101 doi:http://dx.doi.org/10.1107/S2053230X18007689
