YbaK protein domain
| YbaK protein domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure of Cysteinyl-tRNA(Pro) deacylase protein from Haemophilus influenzae (hi1434) | |||||||||
| Identifiers | |||||||||
| Symbol | YbaK | ||||||||
| Pfam | PF04073 | ||||||||
| InterPro | IPR007214 | ||||||||
| SCOP2 | 1dbx / SCOPe / SUPFAM | ||||||||
| CDD | cd04332 | ||||||||
| |||||||||
In molecular biology, this protein domain of unknown function is found in numerous prokaryote organisms. This domain also occurs in a number of prolyl-tRNA synthetases (proRS) from prokaryotes. Thus, the domain is thought to be involved in oligonucleotide binding, with possible roles in recognition/discrimination or editing of prolyl-tRNA.[1]
Function
[edit | edit source]Studies have shown that YbaK functions as a Cys-tRNAPro deacylase in vivo, deacetylation additionally involves turning genes off, hence, it can be assumed that it is preventing the addition of an amino acid to a tRNA molecule, thus preventing translation. In vitro studies with the full set of 20 E. coli aminoacyl-tRNAs revealed that the Haemophilus influenzae and E. coli YbaK proteins are moderately general aminoacyl-tRNA deacylases that preferentially hydrolyze Cys-tRNAPro and Cys-tRNACy. Furthermore, YbaK-mediated hydrolysis of aminoacyl-tRNA has been indicated to influence cell growth.[2] It has been further indicated that YbaK domain is important in the editing function if the wrong amino acid has been joined to the wrong tRNA.
Structure
[edit | edit source]The structure of YbaK shows a novel fold. This domain also occurs in a number of prolyl-tRNA synthetases (proRS) from prokaryotes. Thus, the domain is thought to be involved in oligonucleotide binding, with possible roles in recognition/discrimination or editing of prolyl-tRNA. YbaK is a highly curved mixed seven-stranded beta-sheet surrounded by six short alpha helices[1]