In Silico Structure Modeling and Characterization of Hypothetical Protein YP_004590319.1 Present in Enterobacter aerogens
- *Corresponding Author:
- Ritika Gupta
Department of Biotechnology
Meerut Institute of Engineering and Technology (MIET)
Tel: +91 9703896342
E-mail: [email protected]
Received Date: May 12, 2017; Accepted Date: May 31, 2017; Published Date: June 02, 2017
Citation: Gupta R, Dey A, Vijan A, Gartia B (2017) In Silico Structure Modeling and Characterization of Hypothetical Protein YP_004590319.1 Present in Enterobacter aerogens. J Proteomics Bioinform 10:152-170. doi: 10.4172/jpb.1000436
Copyright: © 2017 Gupta R, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Transfer RNAs anticodon post-transcriptional modifications are responsible to the high fidelity of protein synthesis. In eubacteria, two genome-encoded transfer RNA (tRNA) species bear the same CAU sequence as the anticodons, which are differentiated by modified cytidines at the wobble positions. We have determined the crystal structure of tRNAMet cytidine acetyltransferase (TmcA) from Escherichia coli complexed with two natural ligands, acetyl-CoA and ADP, at 2.35 Å resolutions. The structure unexpectedly reveals an idiosyncratic RNA helicase module fused with a GCN5-related N-acetyltransferase (GNAT) fold, which intimately cross interact. We have unravelled the function of acetyl-CoA as an enzyme-activating switch, and also propose that an RNA helicase motor driven by ATP hydrolysis is used to deliver the wobble base to the active centre of the GNAT domain.