4IWX

Rimk structure at 2.85A

Summary for 4IWX

• Entry DOI: 10.2210/pdb4iwx/pdb
• Related: 4IWY
• Descriptor: Ribosomal protein S6 modification protein, ADENOSINE-5'-DIPHOSPHATE, GLUTAMIC ACID, ... (5 entities in total)
• Functional Keywords: atp-grasp fold, ligase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 35705.51

Authors

Shi, D.,Zhao, G.,Jin, Z.,Allewell, N.M.,Tuchman, M. (deposition date: 2013-01-24, release date: 2013-05-08, Last modification date: 2023-09-20)

Primary citation

Zhao, G.,Jin, Z.,Wang, Y.,Allewell, N.M.,Tuchman, M.,Shi, D.
Structure and function of Escherichia coli RimK, an ATP-grasp fold, l-glutamyl ligase enzyme.
Proteins, 81:1847-1854, 2013

PubMed Abstract: We report herein the crystal structure of Escherichia coli RimK at a resolution of 2.85 Å, an enzyme that catalyzes the post-translational addition of up to 15 C-terminal glutamate residues to ribosomal protein S6. The structure belongs to the ATP-grasp superfamily and is organized as a tetramer, consistent with gel filtration analysis. Each subunit consists of three distinct structural domains and the active site is located in the cleft between these domains. The catalytic reaction appears to occur at the junction between the three domains as ATP binds between the B and C domains, and other substrates bind nearby.

PubMed: 23609986
DOI: 10.1002/prot.24311

Experimental method

X-RAY DIFFRACTION (2.854 Å)