Structural highlights
Function
[LYS_BPT4] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A recently developed method makes it possible to genetically encode unnatural amino acids with diverse physical, chemical or biological properties in Escherichia coli and yeast. We now show that this technology can be used to efficiently and site-specifically incorporate p-iodo-L-phenylalanine (iodoPhe) into proteins in response to an amber TAG codon. The selective introduction of the anomalously scattering iodine atom into proteins should facilitate single-wavelength anomalous dispersion experiments on in-house X-ray sources. To illustrate this, we generated a Phe153 --> iodoPhe mutant of bacteriophage T4 lysozyme and determined its crystal structure using considerably less data than are needed for the equivalent experiment with cysteine and methionine. The iodoPhe residue, although present in the hydrophobic core of the protein, did not perturb the protein structure in any meaningful way. The ability to selectively introduce this and other heavy atom-containing amino acids into proteins should facilitate the structural study of proteins.
The site-specific incorporation of p-iodo-L-phenylalanine into proteins for structure determination.,Xie J, Wang L, Wu N, Brock A, Spraggon G, Schultz PG Nat Biotechnol. 2004 Oct;22(10):1297-301. Epub 2004 Sep 19. PMID:15378068[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xie J, Wang L, Wu N, Brock A, Spraggon G, Schultz PG. The site-specific incorporation of p-iodo-L-phenylalanine into proteins for structure determination. Nat Biotechnol. 2004 Oct;22(10):1297-301. Epub 2004 Sep 19. PMID:15378068 doi:10.1038/nbt1013
