4I9R

Crystal Structure of the R111K:R132L:Y134F:T54V:R59W:A32W Mutant of the Cellular Retinoic Acid Binding Protein Type II in Complex with All-Trans Retinal at 2.6 Angstrom Resolution

Summary for 4I9R

• Entry DOI: 10.2210/pdb4i9r/pdb
• Related: 2FR3 2G78 2G7B 3F8A 3FEP 4EEJ 4EFG 4EXZ 4I9S
• Descriptor: Cellular retinoic acid-binding protein 2, RETINAL (3 entities in total)
• Functional Keywords: protein engineering, wavelength regulation, ph sensing, pka, retinylidene psb, iminium, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P29373
• Total number of polymer chains: 1
• Total formula weight: 15920.37

Authors

Nosrati, M.,Geiger, J.H. (deposition date: 2012-12-05, release date: 2013-10-09, Last modification date: 2024-11-06)

Primary citation

Berbasova, T.,Nosrati, M.,Vasileiou, C.,Wang, W.,Lee, K.S.,Yapici, I.,Geiger, J.H.,Borhan, B.
Rational Design of a Colorimetric pH Sensor from a Soluble Retinoic Acid Chaperone.
J.Am.Chem.Soc., 135:16111-16119, 2013

PubMed Abstract: Reengineering of cellular retinoic acid binding protein II (CRABPII) to be capable of binding retinal as a protonated Schiff base is described. Through rational alterations of the binding pocket, electrostatic perturbations of the embedded retinylidene chromophore that favor delocalization of the iminium charge lead to exquisite control in the regulation of chromophoric absorption properties, spanning the visible spectrum (474-640 nm). The pKa of the retinylidene protonated Schiff base was modulated from 2.4 to 8.1, giving rise to a set of proteins of varying colors and pH sensitivities. These proteins were used to demonstrate a concentration-independent, ratiometric pH sensor.

PubMed: 24059243
DOI: 10.1021/ja404900k

Experimental method

X-RAY DIFFRACTION (2.6 Å)