Structural highlights
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 metal-ion chelating amino acid, (8-hydroxyquinolin-3-yl)alanine, was genetically encoded in E. coli by an amber nonsense codon and corresponding orthogonal tRNA/aminoacyl-tRNA synthetase pair. The amino acid was incorporated into TM0665 protein, and the mutant protein was cocrystallized with Zn(2+) to determine the structure by SAD phasing. The structure showed a high occupancy of the heavy metal bound to the HQ-Ala residue, and the heavy metal provided excellent phasing power to determine the structure. This method also facilitates the de novo design of metalloproteins with novel structures and functions, including fluorescent sensors.
Genetic Incorporation of a Metal-Ion Chelating Amino Acid into Proteins as a Biophysical Probe.,Lee HS, Spraggon G, Schultz PG, Wang F J Am Chem Soc. 2009 Feb 4. PMID:19193005[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee HS, Spraggon G, Schultz PG, Wang F. Genetic Incorporation of a Metal-Ion Chelating Amino Acid into Proteins as a Biophysical Probe. J Am Chem Soc. 2009 Feb 4. PMID:19193005 doi:10.1021/ja808340b
