4QGX

Crystal structure of the R132K:R111L:L121E mutant of Cellular Retinoic Acid Binding ProteinII complexed with a synthetic ligand (Merocyanine) at 1.47 angstrom resolution

Summary for 4QGX

• Entry DOI: 10.2210/pdb4qgx/pdb
• Related: 2G7B 3F8A 3FEP 4EEJ 4EXZ 4I9S 4QGV 4QGW
• Descriptor: Cellular retinoic acid-binding protein 2, (2E,4E,6E)-3-methyl-6-(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)hexa-2,4-dienal (3 entities in total)
• Functional Keywords: protein engineering, protein fluorescence, merocyanine dyes for fluorescent protein labeling, fluorescent protein tag, merocyanine protonated schiff base iminium, protein binding
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 31318.78

Authors

Nosrati, M.,Yapici, I.,Geiger, J.H. (deposition date: 2014-05-26, release date: 2015-01-28, Last modification date: 2024-10-09)

Primary citation

Yapici, I.,Lee, K.S.,Berbasova, T.,Nosrati, M.,Jia, X.,Vasileiou, C.,Wang, W.,Santos, E.M.,Geiger, J.H.,Borhan, B.
"Turn-on" protein fluorescence: in situ formation of cyanine dyes.
J.Am.Chem.Soc., 137:1073-1080, 2015

PubMed Abstract: Protein reengineering of cellular retinoic acid binding protein II (CRABPII) has yielded a genetically addressable system, capable of binding a profluorophoric chromophore that results in fluorescent protein/chromophore complexes. These complexes exhibit far-red emission, with high quantum efficiencies and brightness and also exhibit excellent pH stability spanning the range of 2-11. In the course of this study, it became evident that single mutations of L121E and R59W were most effective in improving the fluorescent characteristics of CRABPII mutants as well as the kinetics of complex formation. The readily crystallizable nature of these proteins was invaluable to provide clues for the observed spectroscopic behavior that results from single mutation of key residues.

PubMed: 25534273
DOI: 10.1021/ja506376j

Experimental method

X-RAY DIFFRACTION (1.471 Å)