Structural highlights
Function
[E8XBD7_SALT4] Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (By similarity).[HAMAP-Rule:MF_01445]
Publication Abstract from PubMed
YgjD from COG0533 is amongst a small group of highly conserved proteins present in all three domains of life. Various roles and biochemical functions (including sialoprotease and endonuclease activities) have been ascribed to YgjD and orthologs, the most recent, however, is involvement in the post transcriptional modification of certain tRNAs by formation of N6-threonyl-adenosine (t6 A) at position 37. In bacteria, YgjD is essential and along with YeaZ, YjeE and YrdC has been shown to be 'necessary and sufficient' for the tRNA modification. To further define interactions and possible roles for some of this set of proteins we have undertaken structural and biochemical studies. We show that formation of the previously reported heterodimer of YgjD-YeaZ involves ordering of the C-terminal region of YeaZ which extends along the surface of YgjD in the crystal structure. ATPgammaS or AMP are observed in YgjD whilst no nucleotide is bound on YeaZ.
Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD-YeaZ-YjeE complex.,Nichols CE, Lamb HK, Thompson P, Omari KE, Lockyer M, Charles I, Hawkins AR, Stammers DK Protein Sci. 2013 Mar 8. doi: 10.1002/pro.2247. PMID:23471679[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nichols CE, Lamb HK, Thompson P, Omari KE, Lockyer M, Charles I, Hawkins AR, Stammers DK. Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD-YeaZ-YjeE complex. Protein Sci. 2013 Mar 8. doi: 10.1002/pro.2247. PMID:23471679 doi:http://dx.doi.org/10.1002/pro.2247
