5ZCT

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

Summary for 5ZCT

Entry DOI	10.2210/pdb5zct/pdb
Descriptor	Ribosomal protein S6--L-glutamate ligase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
Functional Keywords	l-amino acid ligase, ligase
Biological source	Escherichia coli (strain K12)
Total number of polymer chains	8
Total formula weight	270422.92
Authors	Arimura, Y.,Kono, T.,Kino, K.,Kurumizaka, H. (deposition date: 2018-02-20, release date: 2018-07-25, Last modification date: 2025-09-17)
Primary citation	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, 74:385-390, 2018 Cited by PubMed Abstract: Bacterial RimK is an enzyme that catalyzes the polyglutamylation of the C-terminus of ribosomal protein S6 and the synthesis of poly-α-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 Å 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-α-L-glutamate peptides and the polyglutamylation of ribosomal protein S6. PubMed: 29969101 DOI: 10.1107/S2053230X18007689 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.05 Å)

Structure validation