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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function of your protein
Pyrrolysyl-tRNA synthase (PylRS) is a protein found in anaerobic archaea and bacteria. PylRS facilitates the installation of pyrrolysine. It binds to the pyrrolysine substrate. This protein has two functional domains. It has a C-terminus, which is the catalytic domain (PylSc) and has a Rossmann fold, which is a tertiary fold that binds to nucleotides. The other functional domain is the N-terminus that does the tRNA binding (PylSn). These two functional domains can work together to install two noncanonical amino acids at the same time.
There are three types of ligands in this protein, , (Pyrophosphate 2-) and EDO (1,2-ethanediol).
Biological relevance and broader implications
This protein is able to install noncanonical amino acids (ncAAs), amino acids that are found in organisms naturally or are synthetically made in a laboratory. These amino acids are not located in the genetic code of naturally occurring organisms, though. The importance of this protein is that it could be used as a tool for the expansion of genetic code. Since it can install ncAAs into many proteins, it can be sued in many organisms. The protein minimizes the suppression of UAG codons, which code to end a polypeptide chain. This means it can stop the end of that chain and help the expansion of the genetic code.
Important amino acids
Structural highlights
PylRS has two domains, an N-terminal and a C-terminal. The N-terminal is responsible for tRNA-binding, PylSn. The C-terminal is the catalytic domain, PylSc.
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
