Structural highlights
Function
RIMK_ECOLI Responsible for the addition of glutamate residues to the C-terminus of ribosomal protein S6.
Publication Abstract from PubMed
We report herein the crystal structure of E. coli RimK at 2.85 A resolution, an enzyme that catalyzes the post-translational addition of up to fifteen 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 since ATP binds between the B and C domains, and other substrates bind nearby. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc.
Structure and function of Escherichia coli RimK, an ATP-grasp fold, L-glutamyl ligase enzyme.,Zhao G, Jin Z, Wang Y, Allewell NM, Tuchman M, Shi D Proteins. 2013 Apr 23. doi: 10.1002/prot.24311. PMID:23609986[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao G, Jin Z, Wang Y, Allewell NM, Tuchman M, Shi D. Structure and function of Escherichia coli RimK, an ATP-grasp fold, L-glutamyl ligase enzyme. Proteins. 2013 Apr 23. doi: 10.1002/prot.24311. PMID:23609986 doi:http://dx.doi.org/10.1002/prot.24311
