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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.

YLY is the ligand of interest in this enzyme. There are two smaller ligands as well, POP (Pyrophosphate 2-) and EDO (1,2-ethanediol).

Biological relevance and broader implications

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

1. ↑ 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
2. ↑ 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