5zct | pdb_00005zct

The crystal structure of the poly-alpha-L-glutamate peptides synthetase RimK at 2.05 angstrom resolution.

spinqualitylabelsall models 5zct, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zct is a 8 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: ANP, MG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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